International School of Crystallography - Erice
Ettore Majorana Foundation and Centre for Scientific Culture
President: Professor Antonino Zichichi
INTERNATIONAL SCHOOL of CRYSTALLOGRAPHY
Director: Sir Tom Blundell, FRS FMedSci
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Ettore Majorana Foundation and Centre for Scientific Culture
President: Professor Antonino Zichichi
Director: Sir Tom Blundell, FRS FMedSci
Brigham Young University, Provo, UT, US
Institut Laue-Langevin, Grenoble, FR
University of the Basque Country, Bilbao, ES
Since the first magnetic neutron-diffraction experiments almost 70 years ago (1994 Nobel Prize), magnetic-structure research has grown tremendously within the materials physics, chemistry, and engineering fields (e.g. superconductivity, multiferroics, spintronics, information storage, molecular magnetism). Magnetic degrees of freedom lie at the heart of much of the exciting science being done today at international scattering facilities, and hundreds of magnetic structures are now published every year by a diverse range of research communities. In response to this progress, the crystallographic community is also rapidly developing and delivering new infrastructure with which to solve, refine, analyze and describe magnetic structures. Where chaos once reigned, consensus and remarkable new tools have emerged.
The School will address key advances in magnetic-structure research, as well as the foundational and state-of-the-art of theoretical, experimental, and computational capabilities that made these advances possible. The program, which includes both lectures and many hands-on-tutorials, is designed to engage both new and veteran members of the magnetic-structure community. Scientific topics will include:
1) Important magnetic systems and magnetic-structure types (e.g. commensurate and incommensurate, antiferromagnetic, amplitude-modulated, helical, skyrmionic, etc...);
2) The theory and practice of using magnetic symmetry groups (e.g. point groups, space groups, superspace groups, subperiodic groups) and relating them to magnetic physical properties;
3) The complete and unambiguous description of a magnetic structure; comparison of the correct use of wave amplitudes, magnetic supercells, and representational modes; how magnetic symmetry can be used to further constrain any of these descriptions;
4) Advanced instruments and experimental methods for probing magnetic structures;
5) Computational tools for exploring, solving and refining commensurate and incommensurate magnetic structures;
6) Computational tools and resources for performing magnetic representational analyses, applying magnetic symmetry groups, and manipulating the description of a magnetic structure;
7) Open-access archives for commensurate and incommensurate magnetic structures.
Max Avdeev is an instrument scientist responsible for the high-resolution neutron powder diffractometer ECHIDNA at the OPAL research reactor operated by the Australian Nuclear Science and Technology Organisation (ANSTO). He received PhD for synthesis and crystal structural studies of superionic conductors in 1999. Between 2000 and 2005 he worked as a postdoctoral researcher first at the University of Aveiro (Portugal) and then Argonne National Laboratory (USA). In 2005 he joined ANSTO as a full-time scientist. His main research interests are studies of crystal and magnetic structure of inorganic materials using X-ray and neutron diffraction and atomistic modelling.
Laura Cañadillas Delgado was born in Tenerife, Canary Islands (Spain). She was graduated in Physics (2003) and obtained her PhD in Physics (2008) by University of La Laguna. During her PhD work, Laura synthesized, measured and resolved the crystal structure of an important number of metal-organic lanthanide complexes, in the challenge to relate their structures with their magnetic behaviour.
In 2009, she obtained the MICINN fellowship: "Especialización en Organismos Internacionales" which was developed at the European Synchrotron Radiation Facility (Grenoble, France) to investigate at the BM16 beamline. During this period, she managed several experiments in the station adapted for Macromolecular Crystallography. At the end of 2009 she joined the Instituto de Ciencia de Materiales de Aragón (CSIC) in the SpINS group at the Institut Laue Langevin (Grenoble, France) where she specialized in neutron diffraction. During two years, she was in charge of the neutron diffractometers for single crystals (D15) and powder samples (D1B).
Nowadays she is working at the Centro Universitario de Defensa de Zaragoza (CUD) teaching physics and mechanics in the degree Industrial Organization Engineering, and works as scientist in the single crystal neutron diffractometer D19 at ILL, developing her investigation in magneto-structural correlations on metal-organic multifunctional materials.
Laurent Chapon received is PhD in Montpellier (France) in 2000 and was a post-doctoral fellow at the Argonne National Laboratory (US). In 2002, Laurent moved to the ISIS neutron source (UK) where he worked as an instrument scientist and then leader of the Crystallography group, before joining the ILL (France) as a research fellow and head of the diffraction group. In 2016, Laurent Chapon was appointed director of Physical Sciences at the Diamond Light Source (UK) and visiting Professor at Oxford University. His scientific interests lie in studying the magnetic properties of complex magnetic oxides, mostly multiferroics, frustrated systems, and more recently iridates. Having worked in large scale facilities for the last 18 years, Laurent has extended expertise in neutron scattering, including 3D-polarimetry, and magnetic X-ray scattering as well as magnetic crystallography.
Luis Elcoro studied Physics at the Universidad Autonoma in Madrid. During his Ph. D. at the University of the Basque Country he focused on the structure determination of quasicrystals under the superspace formalism. Later he extended the use of the superspace to the analysis of families of compounds whose structure details depend on continuous parameters and to the ordered distributions of vacancies. Since 2011 he is one of the developers of the Bilbao Crystallographic Server (BCS). Most of his contributions to the BCS are included in the Magnetic section, devoted to the structure analysis of magnetic structures based on symmetry considerations. At present he is involved in the study of topological insulators using group theory to describe systematically the electronic extended states (band structures). He is also applying the developed methods to the identification of materials that can potentially be topological insulators or semi-metals.
Oscar Fabelo (b. 1978) graduated in Physics at the Universidad de La Laguna, Spain. He did the PhD in the Physics department (2008) at the same University. During this period he was working as technician in the magnetic measurements service of the Universidad de La Laguna, where he took the first contact with the research on magnetism. During the PhD he carried out several stays at Instituto de Ciencia Molecular (ICMol), Valencia (Spain) to improve his background in molecular magnetism. After the PhD from 2009 to 2014, he worked as scientist in the Instituto de Ciencia de Materiales de Aragon (ICMA), Zaragoza (Spain). During this period he was instrument scientist of the neutron powder diffractometer D1B at Institut Laue Langevin, Grenoble (France). Since 2014 he is responsible for the hot-neutron single crystal diffractometer D9 at the ILL.
His research interests are focused on small molecule crystallography, in particular magneto-structural correlations in coordination polymers and hybrid materials. He have an extensive experience on the field of neutron diffraction in both powder and single crystal.
Ovidiu Garlea is instrument scientist at the HYSPEC spectrometer at the Spallation Neutron Source (SNS), Oak Ridge National Laboratory. He holds a courtesy appointment with the Department of Chemistry and Biochemistry at Florida State University and is adjoint associate professor at the Department of Materials Sciences and Engineering at the University of Tennessee. He received his PhD in solid state physics from Joseph-Fourier University, Grenoble, France in 2001. Since then he has worked as a post-doctoral researcher at the Synchrotron Light Laboratory ELETTRA, at the Ames Laboratory, and at the Oak Ridge National Laboratory. From 2007 until 2013, he served as lead instrument scientist at the HB2A Neutron Powder Diffractometer at High Flux Isotope Reactor (HFIR) where he oversaw the installation of the instrument and built a vibrant magnetic diffraction community. He initiated a workshop series on magnetic structure determination that runs regularly since 2009. Starting with 2013, he contributed to the successful commissioning of the HYSPEC spectrometer at the SNS and to the implementation of the neutron polarization analysis capability. His research focuses on studies of frustrated magnets, quantum systems and strongly correlated electron systems using neutron diffraction and inelastic neutron scattering technique.
Margarida Henriques was born in Coimbra, Portugal and graduated in Materials Engineering at the University of Coimbra. She worked as a Materials Engineer before she obtained her PhD degree in Materials Science and Engineering from the University of Lisbon, Portugal. Her interest in new magnetic crystallography and electronic properties of new materials lead her for her post-doc work within the group of Structure Analysis of the Institute of Physics, Czech Academy of Sciences. She is involved in the development of the magnetic option of Jana2006, which concerns systematic data processing and solution of commensurate and incommensurate magnetic structures. She also works in synthesis and characterization of new materials containing f-elements using x-ray and neutron scattering techniques under multi-extreme conditions. As a part of this work, she stayed at Institute Laue-Langevin in Grenoble, France. There she worked as a scientist in the Diffraction group, studying magnetic diffraction in single-crystals of magnetically frustrated materials.
Margarida is also involved in the preparation and lecturing in workshops concerning the magnetic option of Jana2006 for scientists and students of worldwide renown neutron facilities and lecturing PhD students in Physics at Charles University in Prague. She is also a member of the Comission for Magnetic Structures of IUCR.
Dmitry Khalyavin is a beam-line scientist at the ISIS Facility, pulsed neutron and muon source at the Rutherford Appleton Laboratory (Oxford, UK). He is responsible for the high-resolution cold-neutron diffractometer WISH primarily designed to study large unit cell systems and magnetic ordering in solids. Dmitry joined ISIS in 2008 after completion of his postdoctoral activity at University of Aveiro (Aveiro, Portugal) and Joint Institute for Nuclear Research (Dubna, Russia). He got his PhD degree in condensed matter physics at the Institute of Solid State Physics and Semiconductors of National Academy of Science of Belarus (Minsk, Belarus) in 2002. The main research interest is phase transitions and physical crystallography with a particular focus on magnetic structure determination and crystal structure effects associated with magnetic ordering. Dmitry is deeply involved into the ISIS international user scientific program combined with his own strong research scheme in the field of geometrically frustrated magnetism, multiferroics, iron-based superconductors, heavy fermion metals and Kondo semiconductors.
Václav Petříček studied physics mathematics and physics at the Charles University in Praha. From 1972 till now he works at the Institute of Physics of the Czech Academy of Sciences in Praha. During his one year’s stay in Philip Coppens’s lab he wrote the first version of the program Jana for refinement of modulated structures. Nowadays, after 30 years of development, program JANA serves to about 2000 users as a multi-purpose crystallographic package and it receives 300 citations every year. The latest JANA supports also powder diffraction data, simultaneous refinement against various data sets (powders, single crystals) and radiation sources (x-rays, neutrons, electrons), Time-of-Flight neutron diffraction data and refinement of symmetry deformation modes. The latest research of VP is oriented towards magnetic structures, which can be described using the superspace formalism similarly like modulated structures. The “Crystallographic approach” to magnetic structures has attracted many users from the field. VP also collaborates with his colleague Lukas Palatinus on implementation of refinement procedures for electron diffraction tomography data based on the dynamical theory of diffraction.
For his scientific contribution he has been awarded by ICDD Barrett award in 2013 and the ECA Max Perutz prize in 2016.
Juan Rodriguez-Carvajal has a long experience in diffraction physics of neutrons and x-rays. He is an experimentalist with a strong component in computing and theoretical aspects of diffraction. He got his PhD at the University of Barcelona in 1984 and held different teaching positions in two universities of Barcelona. He got a position as a scientist researcher at the CSIC in the Materials Science Institute of Barcelona. From 1988 to 1994 he was Physicist at the ILL. From 1994 to 2006 he was working at the LLB and he came back to the ILL to lead the Diffraction Group. He has been involved in large scale projects for developing new neutron sources. He has participated in many committees and selection panels for research projects. He has also a strong activity in training worldwide young researchers through many courses on diffraction and crystallography.
JRC's interests:
1. Data analysis and software development in Crystallography and Diffraction Physics.
2. Theoretical analysis of magnetic Structures. Frustration and low dimensional magnetism.
3. Physics of superconducting oxides, intermetallics, metal-Insulator transitions and magnetic ordering. Structural and magnetic aspects of oxides presenting colossal magnetoresistance, charge, spin and orbital ordering phenomena. Energy materials, and multiferroics.
Author of more than 430 papers in scientific journals and books. The number of article citations is more than 17800 (Web of Science), 28000 (Google Scholar).
"Award for Distinguished Powder Diffractionist" from the International Committee of EPDIC (Warsaw, 2008), Barrett Award 2011 of the Denver X-ray Conference for “exceptional contributions to powder diffraction”.
Author of FULLPROF, one of the most used powder diffraction computer programs in the world.
Taku J Sato is presently a full professor at Institute of Multidisciplinary Research for Advanced Materials (IMRAM), Tohoku University (Japan). He obtained his MSc from the Department of Physics, Tokyo Institute of Technology (1993), and received his PhD from the Department of Physics, University of Tokyo (1996). In 1996, he became a staff scientist at National Institute for Metals in Tsukuba, Japan, and then in 2004 he moved to University of Tokyo as an associate professor. From 2012, he has been at Tohoku University. His main research interest is nontrivial macroscopic quantum phenomena in quantum spin systems, including topological spin textures in the real space, emergent quasiparticles in the quantum disordered state, and so on. His expertise is neutron scattering, and has been an instrument scientist on various spectrometers including backscattering spectrometer, triple-axis spectrometer, and direct geometry chopper spectrometers. He has been a commission member for the magnetic structures of IUCr from 2011.
Harold T. Stokes received a PhD in physics in 1977 at the University of Utah where he developed pulsed-NMR double-resonance techniques for studying atomic diffusion in multi-spin crystals. He then spent three years as a post-doc at the University of Illinois applying pulsed NMR to the study of heterogeneous catalysis. In 1981, he joined the faculty in the Department of Physics & Astronomy at Brigham Young University. Three years later, he began a career-long collaboration with Dorian Hatch, and later with Branton Campbell, applying computational group-representation theory to the study of structural phase transitions in crystals. A key product of this effort has been the development of the ISOTROPY Software Suite of online software tools, including the ISODISTORT program. These tools make it possible to conveniently generate and explore the order parameters that arise in phase transitions, and to parameterize them in terms of symmetry modes (basis functions of irreducible representations). The ISOTROPY suite has been a leading contributor of infrastructure for the analysis of commensurate and incommensurate magnetic structures during the past decade.
Dr. Von Dreele has a BS Chem. E. (1966), and PhD Inorganic Chem. (1971), from Cornell. He was Professor of Chemistry at Arizona State University (1971-1986) and a NSF postdoctoral fellow at the ICL, Oxford University (1972-3) where he began his pursuit of powder diffraction crystallography. He was at Los Alamos National Laboratory (1986-2003) as Instrument Scientist for two neutron powder diffractometers, a Fulbright Fellow at the ISIS neutron scattering facility (1986), received a Los Alamos National Laboratory Distinguished Performance Award (1998), presented the 5th Joseph Morgan Lecture at Texas Christian University (2000), and a Fellow of the MSA since 2001. In 2003 he joined Argonne National Laboratory with a joint appointment between IPNS and APS; in early 2008 he became full time at the APS. He was President of the ACA (2009), received the Barrett (2009) and Hanawalt Awards (2013).
Since 1985, Dr. Von Dreele has developed the widely used software, GSAS, for analysis of both neutron and x-ray powder diffraction data; this package has been cited more than 8000 times. He is the author of some 150 publications which includes the 1st protein structure solved from x-ray powder diffraction data. Most recently he has been developing GSAS-II, a replacement for GSAS with a fully integrated GUI, display graphics and computational analysis system for diffraction data.
His main research interests are the development of x-ray and neutron powder diffraction and its application to a wide variety of scientific problems.
Andrew Wills is Professor in Chemistry at UCL. He joined UCL as a Royal Society Senior Research Fellow in 2002, following undergraduate studies at Oxford University, a Ph.D. from Edinburgh University and positions at McMaster University, the Centre d'Etudes Nucléaires de Grenoble - Commissariat à l'énergie atomique (CENG-CEA), the Centre National de la Recherche Scientifique (CNRS), and the Institut Max von Laue-Paul Langevin (ILL). His research interests are focussed on discovering new magnetic properties and searching for new states of matter. This field crosses the traditional disciplines of chemistry and physics and brings together symmetry theory, materials synthesis, physical property measurement, and research software engineering.
Oksana Zaharko (b. 1966) obtained a Master of Science in Solid State Chemistry (1987)
and a PhD in Chemistry (1990) from the Lviv State University, Ukraine. She worked as
a guest scientist in Laboratories of Crystallography in Warsaw,
University of Mainz, ETH Zürich. Since 1998 she works
at Laboratory for Neutron Scattering and Imaging and is responsible for the single crystal
neutron diffractometer ZeBRa (TriCS) at the Swiss Spallation Neutron Source SINQ,
Paul Scherrer Institut.
Her research interests are frustrated and low-dimensional magnetic
systems, and the field of expertise is in neutron scattering and solving complex magnetic structures.
Sanford Burnham Prebys, La Jolla, CA, US
Baylor College of Medicine, Huston, TX, US
MPI of Molecular Physiology, Dortmund, DE
The 54th course will be the inaugural School on 3D CryoEM image analysis at Erice. 3D Cryo-EM image analysis refers to the current practices in image processing and analysis both for single particle analysis and tomography. The School aims to provide a current snapshot of this evolving field, complete with workshops demonstrating state-of-the art software. We plan have tutorials on the major software packages practiced in the field to give participants a solid introduction to the software so they are better prepared to complete a more in-depth tutorial on their own. The sessions will include: deep learning, map improvement , GPU and data storage, cellular tomography, sub-tomogram averaging, phase plate and automated data collection.
Paul Adams is a Senior Scientist at Lawrence Berkeley National Laboratory and an adjunct Professor in the Department of Bioengineering at the University of California Berkeley. He also is Vice President for Technology at the Joint BioEnergy Institute and Director of LBNL’s Molecular Biophysics & Integrated Bioimaging Division. He earned his doctorate in biochemistry at the University of Edinburgh and undertook postdoctoral work at Yale University. Dr. Adams’ research focuses on the development of new algorithms and methods for structural biology, structural studies of large macromolecular machines, and development of cellulosic biofuels. He leads the development of the Phenix software, through a collaboration with researchers from Los Alamos National Lab, Duke University and Cambridge University. Phenix is used for the automated solution of macromolecular structures using crystallographic methods, and more recently has been extended to structure solution, refinement and validation of models obtained from electron cryo-microscopy
I specialize in what has become to be one of the key “Revolutions” in biology in recent times: Cryogenic Electron Microscopy (cryoEM). This cryoEM "revolution" has been made possible by new developments in instrumentation and in image processing and software; it is, precisely, in the area of information processing where our laboratory has excelled. Indeed, we have opened whole new areas in the field, just naming as examples the successful family of Maximum Likelihood algorithms (developed in Madrid from 2007 to 2011), the very much used EMDataBank (started from the European Union “Bioimage” project that I coordinated), or new methods to calculate local resolution in cryoEM maps, all compiled in our software suites XMIPP and SCIPION. Our current efforts focus on the areas of structural validation and flexibility analysis, two of the most demanding topics in our quest to understand at atomic detail the dynamic of large and flexible biological macromolecules. Naturally, structure is one of the ways to understand biological function, to be necessarily complemented by others, a position that explain our continued efforts in information integration, developing widely used environments like 3DBIONOTES. All our new developments are distributed as public software suites, becoming some of the tools that we use in our role as the Image Processing Center of the European Infrastructure for Structural Biology (Instruct ERIC –for European Research Infrastructure Consortium-).
Daniel Castaño-Díez completed his PhD in Applied Mathematics in Bonn in 2005 with a study on the efficient use of wavelets for representation of surfaces in computer graphics. After moving to EMBL in Heidelbeg, he started working in computational methods for cryo electron tomography, focusing on the use of GPUs for alignment and reconstruction of tomograms. He started the development of the software package Dynamo during his post-doc in the Center for Imaging and Nanoanalytics of the University of Basel (2009-2013). Later, he entered the Max Planck Institute for Brain Research in 2014 as joint Head of the Scientific Computing Unit, working on computational infrastructure for the development of image processing algorihtms. Since 2015, he is a Senior Scientist in the BioEM lab of the University of Basel, where he continues the support and extension of the Dynamo software. His research interests are oriented towards the development of numerical methods for high resolution structure determination in in-situ cryoEM and high throughput content analysis of large tomographic data sets.
I received my B.S. in Chemistry at the National Taiwan University. I focused my senior research on X-ray crystallography for the study of chemical bonding in the laboratory of Yu Wang.
My Ph. D. was obtained at The Ohio State University under Martin Caffrey in the area of lipid mesophase transition mechanisms using the time-resolved x-ray diffraction technique.
I entered the cryo 3D EM field in 1995 studying aquaporin in the group of Alok Mitra and cardiac gap junction in the group of Mark Yeager. These postdoctoral projects at The Scripps Research Institute used the two-dimensional crystallography technique.
I then transitioned into the development of an automated cryo-EM data collection software, called Leginon, and a processing pipeline, called Appion, at the National Resources for Automated Molecular Microscopy (NRAMM) under the directorship of Bridget Carragher and Clint Potter. NRAMM is currently located at the Simons Electron Microscopy Center which is part of the New York Structural Biology Center where I am a Senior Research Scientist and the main developer of Leginon and manager of Appion development.
I currently contribute to the field in development of microscopy operation workflows and software that improve the overall throughput and reduce the EM manager workload.
I received the Hildegard H. Crowley Award for Outstanding Technologist in the Biological Sciences in 2018.
David DeRosier received his BS (physics, 1961) in 1961 and his PhD (biophysics, 1965) from the University of Chicago. From 1965-9 he was a postdoctoral fellow with Sir Aaron Klug at the MRC Laboratory of Molecular Biology (Cambridge, England). He and Sir Aaron introduced the method of reconstructing three-dimensional images from electron micrographs and applied it to the helical T4 phage tail. With RA Crowther and LA Amos, they carried out the first single particle reconstructions of two icosahedral viruses. In 1969 DeRosier was hired as assistant professor of chemistry at the University of Texas, Austin. In 1973, he moved becoming associate professor of physics at Brandeis University. In 1979, he became professor of biology at Brandeis. There he developed new methods of image analysis and applied them to the actin cytoskeleton and the bacterial flagellum. He retired in 2005 but continued research in super-resolution light microscopy with Professor G. Turrigiano (Brandeis). In 2015, he became visiting scientist in the Hanein/Volkmann labs at the Burnham (La Jolla, CA). DeRosier received the Elisabeth Roberts Cole Award (Biophysical Society), the Hollaender Award (National Academy of Sciences), and the Distinguished Scientist Award (The Microscopical Society). He is a fellow of the Biophysical Society, the American Academy of Microbiology, the American Association for the Advancement of Science, the American Academy of Arts and Sciences, and the National Academy of Sciences.
Friedrich Förster studied physics at the RWTH University Aachen (Germany, 1995-2000). During his Ph.D. work at the Max-Planck Institute of Biochemistry (Martinsried, Germany) he used cryo-electron tomography (ET) to study the structures of membrane-associated complexes, pioneering subtomogram averaging as a means to increase resolution (2001-2005). After a postdoctoral stay at the University of California San Francisco focusing on integrative modelling of complexes (2005-2008), he started a research group back at Martinsried. Main themes of the group were the structural characterization of protein biogenesis and degradation at organelle membranes and the development of the necessary cryo-ET software. Since 2016, he is a professor at Utrecht University (Netherlands), continuing these research themes.
Most important achievements include (i) developing the first method for subtomogram averaging, (ii) achieving subnanometer resolution for the in situ structure of an asymmetrical complex (ER-associated ribosome) and (iii) determining the atomic structure of the complete 26S proteasome by an integrative approach. He received a Human Frontiers Career Development Award (2012), an ERC Consolidator Grant (2016) and an NWO Vici award (2017) for his research.
Joachim Frank is a Professor of the Department of Biochemistry and Molecular Biophysics, and a Professor of the Department of Biological Sciences at Columbia University. He received his Ph.D. from the Technical University in Munich and, in 1975, joined the Wadsworth Center in Albany as a Senior Research Scientist and, in 1985, joined the faculty of the Department of Biomedical Sciences in the newly founded School of Public Health of SUNY Albany. In 2008 he moved to New York to assume his current positions. Dr. Frank's lab has developed techniques of electron microscopy and single-particle reconstruction of biological macromolecules. He has applied this technique of visualization to explore the structure and dynamics of the ribosome during the process of protein synthesis.
Dr. Frank is a member of the National Academy of Sciences and of the American Academy of Microbiology. He is also a fellow of the American Academy of Arts and Sciences and of the American Association for the Advancement of Science. He was recently honored for his contributions to the development of cryogenic electron microscopy of biological molecules and the study of protein synthesis with the 2014 Franklin Medal for Life Science. In 2017 he shared the Wiley Prize in Biomedical Sciences with Richard Henderson and Marin van Heel, and the Nobel Prize in Chemistry with Richard Henderson and Jacques Dubochet.
Christos Gatsogiannis obtained his PhD in 2009 at the Johannes Gutenberg University of Mainz, Germany. During this time, he worked with Prof. Jürgen Markl on the structure and function of oxygen transporters and was fellow of the German Research Foundation (DFG). This was followed by a four-year postdoctoral period with Prof. Stefan Raunser at the Max Planck Institute of Molecular Physiology in Dortmund as a stipend of the Max Planck Society. There he investigated the structure of a pore forming bacterial toxin, known as ABC, and revealed a novel mechanism of pore formation and protein translocation. In 2015, following a brief post doctoral term at the Free University of Berlin, Gatsogiannis returned to the Max Planck Institute of Molecular Physiology, joining the research staff there. Since 2016, he is a tenured group leader at the institute. The main focus of his group is on the structural analysis of the peroxisomal import machinery and development of new sample preparation methods for high-resolution cryoEM studies of membrane proteins.
Nikolaus Grigorieff (niko@grigorieff.org) studied physics at the Technical University of Berlin (Germany) and Bristol University (UK) and obtained his Ph.D. in 1993. As part of his specialization in solid-state physics, he was trained in high-resolution electron microscopy. This enabled him to move to the Medical Research Council Laboratory of Molecular Biology in Cambridge (UK) as a postdoc to study the structure of biological macromolecules using electron cryo-microscopy. In 1999, he accepted a faculty position at Brandeis University (Waltham, Massachusetts) in the Department of Biochemistry. He became an investigator of the Howard Hughes Medical Institute in 2000 and moved to their Janelia Research Campus in Ashburn (Virginia) in 2013 where he is currently a group leader.
Ben Himes studied Physics and Bioengineering at the Pennsylvania State University where he put theory into practice while investigating the structure of chromatin at the Penn State center for Eukaryotic Gene Regulation. He earned a PhD in Molecular Biophysics at the University of Pittsburgh School of Medicine, where he developed the software package emClarity in the lab of Peijun Zhang. Ben has a strong interest in teaching and during this decade of study spent two years as a Physics TA, worked to design a graduate course in Electron Microscopy, and ran a decent side-hustle tutoring everything from Math to Public speaking. He is now a Postdoctoral Associate at HHMI’s Janelia research campus working under the tutelage of Niko Grigorieff. There he is joining Tim Grant, Alexis Rohou and Niko in developing the software package cisTEM as well as investigating data collection approaches to optimize particle detection in crowded environments. To tilt, or not to tilt, that is the question! Pre-compiled binaries and documentation can be downloaded for cisTEM at https://cistem.org/ and for emClarity at https://github.com/bHimes/emClarity/wiki.
Grant Jensen is an Investigator of the Howard Hughes Medical Institute and a Professor of Biology and Biophysics at the California Institute of Technology in Pasadena, California. He earned his doctorate working on electron microscopy of RNA polymerase and other protein complexes with Dr. Roger Kornberg (who later won the Nobel prize for structural studies of transcription). Next Grant continued his work in protein electron microscopy as a Damon Runyon-Walter Winchell post-doctoral fellow under the supervision of Dr. Kenneth Downing at the Lawrence Berkeley National Lab. Here his interests expanded to include electron tomography of whole cells. Grant launched his own lab at Caltech starting in 2002. At Caltech his research has focused on three main areas: the ultrastructure of small cells, the structural biology of HIV, and the further development of cryo-EM technology. Together with his colleagues he has now published nearly 150 papers in these areas (see http://www.jensenlab.caltech.edu/publications.html). His lab has developed a searchable tomography database and populated it with ~30 thousand cryotomograms of over 100 different viral and microbial samples. Among his most prominent discoveries has been the structure and function of the bacterial type VI secretion system, a "poison-tipped spring-loaded molecular dagger," and the architecture of the type IV pilus responsible for cell motility. All this work has led to the creation of a soon-to-be-released textbook in microbiology, the “Atlas of Bacterial and Archaeal Cell Structure”. Meanwhile his teaching has centered on biophysical methods, including most recently the creation of a popular 14-hour online course "Getting started in Cryo-EM."
Slavica Jonic (slavica.jonic@upmc.fr) received the BSc and MSc degrees in electrical engineering from the University of Belgrade, Serbia, in 1996 and 1999, respectively; the PhD degree in image processing from the Swiss Federal Institute of Technology in Lausanne - EPFL, Switzerland, in 2003; and a Research Director Habilitation from the University Pierre and Marie Curie (UPMC) – Paris 6, France, in 2015.
She held Research and Teaching Assistant positions at the University of Belgrade (1996-1999) and the EPFL (2000-2003), and a Research Scientist position at the UPMC (2004-2008). Since 2008, she is an Associate Scientist (“Chargé de Recherche”) at the French National Centre for Scientific Research (CNRS) and currently with IMPMC-CNRS UMR 7590 at Sorbonne University in Paris, France. Her background is in signal and image processing for biomedical engineering applications such as functional electrical stimulation and computer-assisted surgery. Currently, she works in the area of methods development for the reconstruction of structure and dynamics of biological macromolecular complexes from cryo-electron microscopy images. She is particularly interested in the development of image analysis methods for studying continuous conformational changes of the complexes.
Susan studied medicine at the University of Oxford before undertaking a DPhil with Prof David Stuart using X-ray crystallography to determine the structure of foot and mouth disease viruses. She established her group with a Royal Society Dorothy Hodgkin Fellowship studying human viral-receptor interactions using both X-ray crystallography and electron microscopy. The work of the group gradually moved into work with bacterial pathogens and immune system components leading to her appointment as Chair of Microbiology in the Sir William Dunn School of Pathology, Oxford in 2006. Since 2016 she has been the first Scientific Director of the Central Oxford Structural Microscopy and Imaging Centre driving installation and user training in modern cryo-electron microscopy.
Rafael Fernandez Leiro is a Junior Group Leader at the Spanish National Cancer Research Center (CNIO).
He obtained his PhD in 2011 from the University of A Coruña in Spain where he worked in protein engineering using directed evolution techniques and structure-led rational design. During his PhD, he visited the Rocasolano Institute in Madrid where he was trained in X-ray crystallography. After obtaining the PhD, he joined the Lamers lab at the LMB in Cambridge to work on DNA repair and replication. The timing could not have been better as the cryo-EM “resolution revolution” was happening and the LMB was at the centre of it. For the next six years, he worked with Meindert Lamers and Sjors Scheres to study multiple DNA replication and repair complexes and understand how these systems are regulated using cryo-EM and biochemistry.
He has recently joined CNIO to lead the “Genome Integrity & Structural Biology” group that focuses on the study of the function and biological implications of macromolecular complexes responsible for the maintenance of the integrity of the genome and the role they play in disease.
Cindi Schwartz received her M.S. at the University of Texas, Arlington in 2001. She then worked as a staff scientist in the Boulder Lab for 3D Electron Microscopy of Cells at the University of Colorado under the direction of Dick McIntosh and later Andreas Hoenger until 2014. The Boulder Lab was an NIH Research Resource mandated to accomplish three things: 1) to improve tomography so that other electron microscopy labs could use the technology effectively, 2) to provide tomography services for those who did not have access to the technology, and 3) to disseminate tomography via various training mechanisms to the broader scientific community. In that way, she has been and continues to be an instructor at over 20 workshops and/or conferences where she has taught IMOD and/or SerialEM, the open-source software programs developed by David Mastronarde at the Boulder Lab. Presently, she is a staff scientist under the direction of Elizabeth Fischer at the National Institute of Allergy and Infectious Diseases, Rocky Mountain Laboratories location in Hamilton, Montana. There she continues her work on cryo-electron tomography as well as teaching IMOD and SerialEM. She is an avid supporter of open communication among the scientific community and believes that we can all learn from each other. Therefore she is passionate about teaching and learning from our up-and-coming young scientists who will continue to drive the momentum we currently have in 3D cryo-electron microscopy.
Henning Stahlberg studied Physics at the Technical University of Berlin, and obtained his PhD from the EPFL Lausanne in 2003 in Structural Biology (Groups Prof. Horst Vogel and Prof. Jacques Dubochet). He then obtained his Habilitation in the group of Prof. Andreas Engel at the Biozentrum of the University of Basel in 2008, and accepted in 2009 a faculty position in Molecular and Cell Biology at the University of California in Davis, CA, USA, where he established a laboratory for high-resolution structure determination of biological macromolecules by cryo-transmission electron microscopy. Since 2009, Stahlberg is Professor and director of the Center for Cellular Imaging and NanoAnalytics (C-CINA) of the Biozentrum at the University of Basel.
The Stahlberg group is focusing on Parkinson's Disease and on Membrane Protein Structures. The main method is cryo-electron microscopy, which is extended by multidisciplinary approaches, including use of neuronal cell cultures and human brain tissue, using expression and purification of relevant protein systems, and biophysical and structural investigations with a variety of tools.
We are also developing methods to advance imaging capabilities, ranging from microfluidic cell handling and proteome preparation, to developing instrumentation allowing the preparation of cryo-electron microscopy grids from nanoliters of sample (Braun team).
Dr. Volkmann's research focuses on the development and application of computational tools to bridge information between the atomic and cellular scales, covering more than six orders of magnitude from Ångstroms to tens of microns. Central to this effort is the analysis and interpretation of reconstructions from electron cryo-microscopy (cryo-EM) and cellular electron cryo-tomography (cryo-ET). During his education and career, he acquired a broad background in mathematics, physics, artificial intelligence research, structural and computational biology, and image processing. While at the Max-Planck Institute in Germany in the early 90’s, he carried out experimental and computational aspects of ribosome crystallography under the guidance of Prof. Ada Yonath who won the 2009 Nobel Prize in chemistry. As a postdoctoral fellow at the Keck Center, Brandeis University, Dr. Volkmann expanded his research to include cryo-EM, cryo-ET, and image analysis under the guidance of David DeRosier, one of the founding fathers of three-dimensional reconstruction and analysis techniques.
Dr. Peijun Zhang obtained her Ph.D. in Biophysics and Physiology from University Virginia, M.S. in Physics and B.S. in Electrical Engineering from Nanjing University, China. She was a postdoc and subsequently a staff scientist at the National Cancer Institute, NIH. In 2006, she joined the faculty of the University of Pittsburgh, and was promoted to associate professor with tenure in 2012. She recently joined the University of Oxford as a full professor, and jointly as the founding director of eBIC (the UK National Electron Bio-imaging Centre) at the Diamond Light Source. Her research focuses on the molecular mechanisms of large protein complexes and assemblies, in particular those involved in HIV-1 pathogenesis and bacterial chemotaxis signaling, by developing and combining novel technologies for high-resolution cryoEM and cryoET. She received many awards, including “Carnegie Science Emerging Female Scientist Award” (2014) and “Wellcome Trust Investigator Award” (2017).
Brigham Young University, Provo, UT, US
Institut Laue-Langevin, Grenoble, FR
University of the Basque Country, Bilbao, ES
Since the first magnetic neutron-diffraction experiments almost 70 years ago (1994 Nobel Prize), magnetic-structure research has grown tremendously within the materials physics, chemistry, and engineering fields (e.g. superconductivity, multiferroics, spintronics, information storage, molecular magnetism). Magnetic degrees of freedom lie at the heart of much of the exciting science being done today at international scattering facilities, and hundreds of magnetic structures are now published every year by a diverse range of research communities. In response to this progress, the crystallographic community is also rapidly developing and delivering new infrastructure with which to solve, refine, analyze and describe magnetic structures. Where chaos once reigned, consensus and remarkable new tools have emerged.
The School will address key advances in magnetic-structure research, as well as the foundational and state-of-the-art of theoretical, experimental, and computational capabilities that made these advances possible. The program, which includes both lectures and many hands-on-tutorials, is designed to engage both new and veteran members of the magnetic-structure community. Scientific topics will include:
1) Important magnetic systems and magnetic-structure types (e.g. commensurate and incommensurate, antiferromagnetic, amplitude-modulated, helical, skyrmionic, etc...);
2) The theory and practice of using magnetic symmetry groups (e.g. point groups, space groups, superspace groups, subperiodic groups) and relating them to magnetic physical properties;
3) The complete and unambiguous description of a magnetic structure; comparison of the correct use of wave amplitudes, magnetic supercells, and representational modes; how magnetic symmetry can be used to further constrain any of these descriptions;
4) Advanced instruments and experimental methods for probing magnetic structures;
5) Computational tools for exploring, solving and refining commensurate and incommensurate magnetic structures;
6) Computational tools and resources for performing magnetic representational analyses, applying magnetic symmetry groups, and manipulating the description of a magnetic structure;
7) Open-access archives for commensurate and incommensurate magnetic structures.
Max Avdeev is an instrument scientist responsible for the high-resolution neutron powder diffractometer ECHIDNA at the OPAL research reactor operated by the Australian Nuclear Science and Technology Organisation (ANSTO). He received PhD for synthesis and crystal structural studies of superionic conductors in 1999. Between 2000 and 2005 he worked as a postdoctoral researcher first at the University of Aveiro (Portugal) and then Argonne National Laboratory (USA). In 2005 he joined ANSTO as a full-time scientist. His main research interests are studies of crystal and magnetic structure of inorganic materials using X-ray and neutron diffraction and atomistic modelling.
Laura Cañadillas Delgado was born in Tenerife, Canary Islands (Spain). She was graduated in Physics (2003) and obtained her PhD in Physics (2008) by University of La Laguna. During her PhD work, Laura synthesized, measured and resolved the crystal structure of an important number of metal-organic lanthanide complexes, in the challenge to relate their structures with their magnetic behaviour.
In 2009, she obtained the MICINN fellowship: "Especialización en Organismos Internacionales" which was developed at the European Synchrotron Radiation Facility (Grenoble, France) to investigate at the BM16 beamline. During this period, she managed several experiments in the station adapted for Macromolecular Crystallography. At the end of 2009 she joined the Instituto de Ciencia de Materiales de Aragón (CSIC) in the SpINS group at the Institut Laue Langevin (Grenoble, France) where she specialized in neutron diffraction. During two years, she was in charge of the neutron diffractometers for single crystals (D15) and powder samples (D1B).
Nowadays she is working at the Centro Universitario de Defensa de Zaragoza (CUD) teaching physics and mechanics in the degree Industrial Organization Engineering, and works as scientist in the single crystal neutron diffractometer D19 at ILL, developing her investigation in magneto-structural correlations on metal-organic multifunctional materials.
Laurent Chapon received is PhD in Montpellier (France) in 2000 and was a post-doctoral fellow at the Argonne National Laboratory (US). In 2002, Laurent moved to the ISIS neutron source (UK) where he worked as an instrument scientist and then leader of the Crystallography group, before joining the ILL (France) as a research fellow and head of the diffraction group. In 2016, Laurent Chapon was appointed director of Physical Sciences at the Diamond Light Source (UK) and visiting Professor at Oxford University. His scientific interests lie in studying the magnetic properties of complex magnetic oxides, mostly multiferroics, frustrated systems, and more recently iridates. Having worked in large scale facilities for the last 18 years, Laurent has extended expertise in neutron scattering, including 3D-polarimetry, and magnetic X-ray scattering as well as magnetic crystallography.
Luis Elcoro studied Physics at the Universidad Autonoma in Madrid. During his Ph. D. at the University of the Basque Country he focused on the structure determination of quasicrystals under the superspace formalism. Later he extended the use of the superspace to the analysis of families of compounds whose structure details depend on continuous parameters and to the ordered distributions of vacancies. Since 2011 he is one of the developers of the Bilbao Crystallographic Server (BCS). Most of his contributions to the BCS are included in the Magnetic section, devoted to the structure analysis of magnetic structures based on symmetry considerations. At present he is involved in the study of topological insulators using group theory to describe systematically the electronic extended states (band structures). He is also applying the developed methods to the identification of materials that can potentially be topological insulators or semi-metals.
Oscar Fabelo (b. 1978) graduated in Physics at the Universidad de La Laguna, Spain. He did the PhD in the Physics department (2008) at the same University. During this period he was working as technician in the magnetic measurements service of the Universidad de La Laguna, where he took the first contact with the research on magnetism. During the PhD he carried out several stays at Instituto de Ciencia Molecular (ICMol), Valencia (Spain) to improve his background in molecular magnetism. After the PhD from 2009 to 2014, he worked as scientist in the Instituto de Ciencia de Materiales de Aragon (ICMA), Zaragoza (Spain). During this period he was instrument scientist of the neutron powder diffractometer D1B at Institut Laue Langevin, Grenoble (France). Since 2014 he is responsible for the hot-neutron single crystal diffractometer D9 at the ILL.
His research interests are focused on small molecule crystallography, in particular magneto-structural correlations in coordination polymers and hybrid materials. He have an extensive experience on the field of neutron diffraction in both powder and single crystal.
Ovidiu Garlea is instrument scientist at the HYSPEC spectrometer at the Spallation Neutron Source (SNS), Oak Ridge National Laboratory. He holds a courtesy appointment with the Department of Chemistry and Biochemistry at Florida State University and is adjoint associate professor at the Department of Materials Sciences and Engineering at the University of Tennessee. He received his PhD in solid state physics from Joseph-Fourier University, Grenoble, France in 2001. Since then he has worked as a post-doctoral researcher at the Synchrotron Light Laboratory ELETTRA, at the Ames Laboratory, and at the Oak Ridge National Laboratory. From 2007 until 2013, he served as lead instrument scientist at the HB2A Neutron Powder Diffractometer at High Flux Isotope Reactor (HFIR) where he oversaw the installation of the instrument and built a vibrant magnetic diffraction community. He initiated a workshop series on magnetic structure determination that runs regularly since 2009. Starting with 2013, he contributed to the successful commissioning of the HYSPEC spectrometer at the SNS and to the implementation of the neutron polarization analysis capability. His research focuses on studies of frustrated magnets, quantum systems and strongly correlated electron systems using neutron diffraction and inelastic neutron scattering technique.
Margarida Henriques was born in Coimbra, Portugal and graduated in Materials Engineering at the University of Coimbra. She worked as a Materials Engineer before she obtained her PhD degree in Materials Science and Engineering from the University of Lisbon, Portugal. Her interest in new magnetic crystallography and electronic properties of new materials lead her for her post-doc work within the group of Structure Analysis of the Institute of Physics, Czech Academy of Sciences. She is involved in the development of the magnetic option of Jana2006, which concerns systematic data processing and solution of commensurate and incommensurate magnetic structures. She also works in synthesis and characterization of new materials containing f-elements using x-ray and neutron scattering techniques under multi-extreme conditions. As a part of this work, she stayed at Institute Laue-Langevin in Grenoble, France. There she worked as a scientist in the Diffraction group, studying magnetic diffraction in single-crystals of magnetically frustrated materials.
Margarida is also involved in the preparation and lecturing in workshops concerning the magnetic option of Jana2006 for scientists and students of worldwide renown neutron facilities and lecturing PhD students in Physics at Charles University in Prague. She is also a member of the Comission for Magnetic Structures of IUCR.
Dmitry Khalyavin is a beam-line scientist at the ISIS Facility, pulsed neutron and muon source at the Rutherford Appleton Laboratory (Oxford, UK). He is responsible for the high-resolution cold-neutron diffractometer WISH primarily designed to study large unit cell systems and magnetic ordering in solids. Dmitry joined ISIS in 2008 after completion of his postdoctoral activity at University of Aveiro (Aveiro, Portugal) and Joint Institute for Nuclear Research (Dubna, Russia). He got his PhD degree in condensed matter physics at the Institute of Solid State Physics and Semiconductors of National Academy of Science of Belarus (Minsk, Belarus) in 2002. The main research interest is phase transitions and physical crystallography with a particular focus on magnetic structure determination and crystal structure effects associated with magnetic ordering. Dmitry is deeply involved into the ISIS international user scientific program combined with his own strong research scheme in the field of geometrically frustrated magnetism, multiferroics, iron-based superconductors, heavy fermion metals and Kondo semiconductors.
Václav Petříček studied physics mathematics and physics at the Charles University in Praha. From 1972 till now he works at the Institute of Physics of the Czech Academy of Sciences in Praha. During his one year’s stay in Philip Coppens’s lab he wrote the first version of the program Jana for refinement of modulated structures. Nowadays, after 30 years of development, program JANA serves to about 2000 users as a multi-purpose crystallographic package and it receives 300 citations every year. The latest JANA supports also powder diffraction data, simultaneous refinement against various data sets (powders, single crystals) and radiation sources (x-rays, neutrons, electrons), Time-of-Flight neutron diffraction data and refinement of symmetry deformation modes. The latest research of VP is oriented towards magnetic structures, which can be described using the superspace formalism similarly like modulated structures. The “Crystallographic approach” to magnetic structures has attracted many users from the field. VP also collaborates with his colleague Lukas Palatinus on implementation of refinement procedures for electron diffraction tomography data based on the dynamical theory of diffraction.
For his scientific contribution he has been awarded by ICDD Barrett award in 2013 and the ECA Max Perutz prize in 2016.
Juan Rodriguez-Carvajal has a long experience in diffraction physics of neutrons and x-rays. He is an experimentalist with a strong component in computing and theoretical aspects of diffraction. He got his PhD at the University of Barcelona in 1984 and held different teaching positions in two universities of Barcelona. He got a position as a scientist researcher at the CSIC in the Materials Science Institute of Barcelona. From 1988 to 1994 he was Physicist at the ILL. From 1994 to 2006 he was working at the LLB and he came back to the ILL to lead the Diffraction Group. He has been involved in large scale projects for developing new neutron sources. He has participated in many committees and selection panels for research projects. He has also a strong activity in training worldwide young researchers through many courses on diffraction and crystallography.
JRC's interests:
1. Data analysis and software development in Crystallography and Diffraction Physics.
2. Theoretical analysis of magnetic Structures. Frustration and low dimensional magnetism.
3. Physics of superconducting oxides, intermetallics, metal-Insulator transitions and magnetic ordering. Structural and magnetic aspects of oxides presenting colossal magnetoresistance, charge, spin and orbital ordering phenomena. Energy materials, and multiferroics.
Author of more than 430 papers in scientific journals and books. The number of article citations is more than 17800 (Web of Science), 28000 (Google Scholar).
"Award for Distinguished Powder Diffractionist" from the International Committee of EPDIC (Warsaw, 2008), Barrett Award 2011 of the Denver X-ray Conference for “exceptional contributions to powder diffraction”.
Author of FULLPROF, one of the most used powder diffraction computer programs in the world.
Taku J Sato is presently a full professor at Institute of Multidisciplinary Research for Advanced Materials (IMRAM), Tohoku University (Japan). He obtained his MSc from the Department of Physics, Tokyo Institute of Technology (1993), and received his PhD from the Department of Physics, University of Tokyo (1996). In 1996, he became a staff scientist at National Institute for Metals in Tsukuba, Japan, and then in 2004 he moved to University of Tokyo as an associate professor. From 2012, he has been at Tohoku University. His main research interest is nontrivial macroscopic quantum phenomena in quantum spin systems, including topological spin textures in the real space, emergent quasiparticles in the quantum disordered state, and so on. His expertise is neutron scattering, and has been an instrument scientist on various spectrometers including backscattering spectrometer, triple-axis spectrometer, and direct geometry chopper spectrometers. He has been a commission member for the magnetic structures of IUCr from 2011.
Harold T. Stokes received a PhD in physics in 1977 at the University of Utah where he developed pulsed-NMR double-resonance techniques for studying atomic diffusion in multi-spin crystals. He then spent three years as a post-doc at the University of Illinois applying pulsed NMR to the study of heterogeneous catalysis. In 1981, he joined the faculty in the Department of Physics & Astronomy at Brigham Young University. Three years later, he began a career-long collaboration with Dorian Hatch, and later with Branton Campbell, applying computational group-representation theory to the study of structural phase transitions in crystals. A key product of this effort has been the development of the ISOTROPY Software Suite of online software tools, including the ISODISTORT program. These tools make it possible to conveniently generate and explore the order parameters that arise in phase transitions, and to parameterize them in terms of symmetry modes (basis functions of irreducible representations). The ISOTROPY suite has been a leading contributor of infrastructure for the analysis of commensurate and incommensurate magnetic structures during the past decade.
Dr. Von Dreele has a BS Chem. E. (1966), and PhD Inorganic Chem. (1971), from Cornell. He was Professor of Chemistry at Arizona State University (1971-1986) and a NSF postdoctoral fellow at the ICL, Oxford University (1972-3) where he began his pursuit of powder diffraction crystallography. He was at Los Alamos National Laboratory (1986-2003) as Instrument Scientist for two neutron powder diffractometers, a Fulbright Fellow at the ISIS neutron scattering facility (1986), received a Los Alamos National Laboratory Distinguished Performance Award (1998), presented the 5th Joseph Morgan Lecture at Texas Christian University (2000), and a Fellow of the MSA since 2001. In 2003 he joined Argonne National Laboratory with a joint appointment between IPNS and APS; in early 2008 he became full time at the APS. He was President of the ACA (2009), received the Barrett (2009) and Hanawalt Awards (2013).
Since 1985, Dr. Von Dreele has developed the widely used software, GSAS, for analysis of both neutron and x-ray powder diffraction data; this package has been cited more than 8000 times. He is the author of some 150 publications which includes the 1st protein structure solved from x-ray powder diffraction data. Most recently he has been developing GSAS-II, a replacement for GSAS with a fully integrated GUI, display graphics and computational analysis system for diffraction data.
His main research interests are the development of x-ray and neutron powder diffraction and its application to a wide variety of scientific problems.
Andrew Wills is Professor in Chemistry at UCL. He joined UCL as a Royal Society Senior Research Fellow in 2002, following undergraduate studies at Oxford University, a Ph.D. from Edinburgh University and positions at McMaster University, the Centre d'Etudes Nucléaires de Grenoble - Commissariat à l'énergie atomique (CENG-CEA), the Centre National de la Recherche Scientifique (CNRS), and the Institut Max von Laue-Paul Langevin (ILL). His research interests are focussed on discovering new magnetic properties and searching for new states of matter. This field crosses the traditional disciplines of chemistry and physics and brings together symmetry theory, materials synthesis, physical property measurement, and research software engineering.
Oksana Zaharko (b. 1966) obtained a Master of Science in Solid State Chemistry (1987)
and a PhD in Chemistry (1990) from the Lviv State University, Ukraine. She worked as
a guest scientist in Laboratories of Crystallography in Warsaw,
University of Mainz, ETH Zürich. Since 1998 she works
at Laboratory for Neutron Scattering and Imaging and is responsible for the single crystal
neutron diffractometer ZeBRa (TriCS) at the Swiss Spallation Neutron Source SINQ,
Paul Scherrer Institut.
Her research interests are frustrated and low-dimensional magnetic
systems, and the field of expertise is in neutron scattering and solving complex magnetic structures.
Sanford Burnham Prebys, La Jolla, CA, US
Baylor College of Medicine, Huston, TX, US
MPI of Molecular Physiology, Dortmund, DE
The 54th course will be the inaugural School on 3D CryoEM image analysis at Erice. 3D Cryo-EM image analysis refers to the current practices in image processing and analysis both for single particle analysis and tomography. The School aims to provide a current snapshot of this evolving field, complete with workshops demonstrating state-of-the art software. We plan have tutorials on the major software packages practiced in the field to give participants a solid introduction to the software so they are better prepared to complete a more in-depth tutorial on their own. The sessions will include: deep learning, map improvement , GPU and data storage, cellular tomography, sub-tomogram averaging, phase plate and automated data collection.
Paul Adams is a Senior Scientist at Lawrence Berkeley National Laboratory and an adjunct Professor in the Department of Bioengineering at the University of California Berkeley. He also is Vice President for Technology at the Joint BioEnergy Institute and Director of LBNL’s Molecular Biophysics & Integrated Bioimaging Division. He earned his doctorate in biochemistry at the University of Edinburgh and undertook postdoctoral work at Yale University. Dr. Adams’ research focuses on the development of new algorithms and methods for structural biology, structural studies of large macromolecular machines, and development of cellulosic biofuels. He leads the development of the Phenix software, through a collaboration with researchers from Los Alamos National Lab, Duke University and Cambridge University. Phenix is used for the automated solution of macromolecular structures using crystallographic methods, and more recently has been extended to structure solution, refinement and validation of models obtained from electron cryo-microscopy
I specialize in what has become to be one of the key “Revolutions” in biology in recent times: Cryogenic Electron Microscopy (cryoEM). This cryoEM "revolution" has been made possible by new developments in instrumentation and in image processing and software; it is, precisely, in the area of information processing where our laboratory has excelled. Indeed, we have opened whole new areas in the field, just naming as examples the successful family of Maximum Likelihood algorithms (developed in Madrid from 2007 to 2011), the very much used EMDataBank (started from the European Union “Bioimage” project that I coordinated), or new methods to calculate local resolution in cryoEM maps, all compiled in our software suites XMIPP and SCIPION. Our current efforts focus on the areas of structural validation and flexibility analysis, two of the most demanding topics in our quest to understand at atomic detail the dynamic of large and flexible biological macromolecules. Naturally, structure is one of the ways to understand biological function, to be necessarily complemented by others, a position that explain our continued efforts in information integration, developing widely used environments like 3DBIONOTES. All our new developments are distributed as public software suites, becoming some of the tools that we use in our role as the Image Processing Center of the European Infrastructure for Structural Biology (Instruct ERIC –for European Research Infrastructure Consortium-).
Daniel Castaño-Díez completed his PhD in Applied Mathematics in Bonn in 2005 with a study on the efficient use of wavelets for representation of surfaces in computer graphics. After moving to EMBL in Heidelbeg, he started working in computational methods for cryo electron tomography, focusing on the use of GPUs for alignment and reconstruction of tomograms. He started the development of the software package Dynamo during his post-doc in the Center for Imaging and Nanoanalytics of the University of Basel (2009-2013). Later, he entered the Max Planck Institute for Brain Research in 2014 as joint Head of the Scientific Computing Unit, working on computational infrastructure for the development of image processing algorihtms. Since 2015, he is a Senior Scientist in the BioEM lab of the University of Basel, where he continues the support and extension of the Dynamo software. His research interests are oriented towards the development of numerical methods for high resolution structure determination in in-situ cryoEM and high throughput content analysis of large tomographic data sets.
I received my B.S. in Chemistry at the National Taiwan University. I focused my senior research on X-ray crystallography for the study of chemical bonding in the laboratory of Yu Wang.
My Ph. D. was obtained at The Ohio State University under Martin Caffrey in the area of lipid mesophase transition mechanisms using the time-resolved x-ray diffraction technique.
I entered the cryo 3D EM field in 1995 studying aquaporin in the group of Alok Mitra and cardiac gap junction in the group of Mark Yeager. These postdoctoral projects at The Scripps Research Institute used the two-dimensional crystallography technique.
I then transitioned into the development of an automated cryo-EM data collection software, called Leginon, and a processing pipeline, called Appion, at the National Resources for Automated Molecular Microscopy (NRAMM) under the directorship of Bridget Carragher and Clint Potter. NRAMM is currently located at the Simons Electron Microscopy Center which is part of the New York Structural Biology Center where I am a Senior Research Scientist and the main developer of Leginon and manager of Appion development.
I currently contribute to the field in development of microscopy operation workflows and software that improve the overall throughput and reduce the EM manager workload.
I received the Hildegard H. Crowley Award for Outstanding Technologist in the Biological Sciences in 2018.
David DeRosier received his BS (physics, 1961) in 1961 and his PhD (biophysics, 1965) from the University of Chicago. From 1965-9 he was a postdoctoral fellow with Sir Aaron Klug at the MRC Laboratory of Molecular Biology (Cambridge, England). He and Sir Aaron introduced the method of reconstructing three-dimensional images from electron micrographs and applied it to the helical T4 phage tail. With RA Crowther and LA Amos, they carried out the first single particle reconstructions of two icosahedral viruses. In 1969 DeRosier was hired as assistant professor of chemistry at the University of Texas, Austin. In 1973, he moved becoming associate professor of physics at Brandeis University. In 1979, he became professor of biology at Brandeis. There he developed new methods of image analysis and applied them to the actin cytoskeleton and the bacterial flagellum. He retired in 2005 but continued research in super-resolution light microscopy with Professor G. Turrigiano (Brandeis). In 2015, he became visiting scientist in the Hanein/Volkmann labs at the Burnham (La Jolla, CA). DeRosier received the Elisabeth Roberts Cole Award (Biophysical Society), the Hollaender Award (National Academy of Sciences), and the Distinguished Scientist Award (The Microscopical Society). He is a fellow of the Biophysical Society, the American Academy of Microbiology, the American Association for the Advancement of Science, the American Academy of Arts and Sciences, and the National Academy of Sciences.
Friedrich Förster studied physics at the RWTH University Aachen (Germany, 1995-2000). During his Ph.D. work at the Max-Planck Institute of Biochemistry (Martinsried, Germany) he used cryo-electron tomography (ET) to study the structures of membrane-associated complexes, pioneering subtomogram averaging as a means to increase resolution (2001-2005). After a postdoctoral stay at the University of California San Francisco focusing on integrative modelling of complexes (2005-2008), he started a research group back at Martinsried. Main themes of the group were the structural characterization of protein biogenesis and degradation at organelle membranes and the development of the necessary cryo-ET software. Since 2016, he is a professor at Utrecht University (Netherlands), continuing these research themes.
Most important achievements include (i) developing the first method for subtomogram averaging, (ii) achieving subnanometer resolution for the in situ structure of an asymmetrical complex (ER-associated ribosome) and (iii) determining the atomic structure of the complete 26S proteasome by an integrative approach. He received a Human Frontiers Career Development Award (2012), an ERC Consolidator Grant (2016) and an NWO Vici award (2017) for his research.
Joachim Frank is a Professor of the Department of Biochemistry and Molecular Biophysics, and a Professor of the Department of Biological Sciences at Columbia University. He received his Ph.D. from the Technical University in Munich and, in 1975, joined the Wadsworth Center in Albany as a Senior Research Scientist and, in 1985, joined the faculty of the Department of Biomedical Sciences in the newly founded School of Public Health of SUNY Albany. In 2008 he moved to New York to assume his current positions. Dr. Frank's lab has developed techniques of electron microscopy and single-particle reconstruction of biological macromolecules. He has applied this technique of visualization to explore the structure and dynamics of the ribosome during the process of protein synthesis.
Dr. Frank is a member of the National Academy of Sciences and of the American Academy of Microbiology. He is also a fellow of the American Academy of Arts and Sciences and of the American Association for the Advancement of Science. He was recently honored for his contributions to the development of cryogenic electron microscopy of biological molecules and the study of protein synthesis with the 2014 Franklin Medal for Life Science. In 2017 he shared the Wiley Prize in Biomedical Sciences with Richard Henderson and Marin van Heel, and the Nobel Prize in Chemistry with Richard Henderson and Jacques Dubochet.
Christos Gatsogiannis obtained his PhD in 2009 at the Johannes Gutenberg University of Mainz, Germany. During this time, he worked with Prof. Jürgen Markl on the structure and function of oxygen transporters and was fellow of the German Research Foundation (DFG). This was followed by a four-year postdoctoral period with Prof. Stefan Raunser at the Max Planck Institute of Molecular Physiology in Dortmund as a stipend of the Max Planck Society. There he investigated the structure of a pore forming bacterial toxin, known as ABC, and revealed a novel mechanism of pore formation and protein translocation. In 2015, following a brief post doctoral term at the Free University of Berlin, Gatsogiannis returned to the Max Planck Institute of Molecular Physiology, joining the research staff there. Since 2016, he is a tenured group leader at the institute. The main focus of his group is on the structural analysis of the peroxisomal import machinery and development of new sample preparation methods for high-resolution cryoEM studies of membrane proteins.
Nikolaus Grigorieff (niko@grigorieff.org) studied physics at the Technical University of Berlin (Germany) and Bristol University (UK) and obtained his Ph.D. in 1993. As part of his specialization in solid-state physics, he was trained in high-resolution electron microscopy. This enabled him to move to the Medical Research Council Laboratory of Molecular Biology in Cambridge (UK) as a postdoc to study the structure of biological macromolecules using electron cryo-microscopy. In 1999, he accepted a faculty position at Brandeis University (Waltham, Massachusetts) in the Department of Biochemistry. He became an investigator of the Howard Hughes Medical Institute in 2000 and moved to their Janelia Research Campus in Ashburn (Virginia) in 2013 where he is currently a group leader.
Ben Himes studied Physics and Bioengineering at the Pennsylvania State University where he put theory into practice while investigating the structure of chromatin at the Penn State center for Eukaryotic Gene Regulation. He earned a PhD in Molecular Biophysics at the University of Pittsburgh School of Medicine, where he developed the software package emClarity in the lab of Peijun Zhang. Ben has a strong interest in teaching and during this decade of study spent two years as a Physics TA, worked to design a graduate course in Electron Microscopy, and ran a decent side-hustle tutoring everything from Math to Public speaking. He is now a Postdoctoral Associate at HHMI’s Janelia research campus working under the tutelage of Niko Grigorieff. There he is joining Tim Grant, Alexis Rohou and Niko in developing the software package cisTEM as well as investigating data collection approaches to optimize particle detection in crowded environments. To tilt, or not to tilt, that is the question! Pre-compiled binaries and documentation can be downloaded for cisTEM at https://cistem.org/ and for emClarity at https://github.com/bHimes/emClarity/wiki.
Grant Jensen is an Investigator of the Howard Hughes Medical Institute and a Professor of Biology and Biophysics at the California Institute of Technology in Pasadena, California. He earned his doctorate working on electron microscopy of RNA polymerase and other protein complexes with Dr. Roger Kornberg (who later won the Nobel prize for structural studies of transcription). Next Grant continued his work in protein electron microscopy as a Damon Runyon-Walter Winchell post-doctoral fellow under the supervision of Dr. Kenneth Downing at the Lawrence Berkeley National Lab. Here his interests expanded to include electron tomography of whole cells. Grant launched his own lab at Caltech starting in 2002. At Caltech his research has focused on three main areas: the ultrastructure of small cells, the structural biology of HIV, and the further development of cryo-EM technology. Together with his colleagues he has now published nearly 150 papers in these areas (see http://www.jensenlab.caltech.edu/publications.html). His lab has developed a searchable tomography database and populated it with ~30 thousand cryotomograms of over 100 different viral and microbial samples. Among his most prominent discoveries has been the structure and function of the bacterial type VI secretion system, a "poison-tipped spring-loaded molecular dagger," and the architecture of the type IV pilus responsible for cell motility. All this work has led to the creation of a soon-to-be-released textbook in microbiology, the “Atlas of Bacterial and Archaeal Cell Structure”. Meanwhile his teaching has centered on biophysical methods, including most recently the creation of a popular 14-hour online course "Getting started in Cryo-EM."
Slavica Jonic (slavica.jonic@upmc.fr) received the BSc and MSc degrees in electrical engineering from the University of Belgrade, Serbia, in 1996 and 1999, respectively; the PhD degree in image processing from the Swiss Federal Institute of Technology in Lausanne - EPFL, Switzerland, in 2003; and a Research Director Habilitation from the University Pierre and Marie Curie (UPMC) – Paris 6, France, in 2015.
She held Research and Teaching Assistant positions at the University of Belgrade (1996-1999) and the EPFL (2000-2003), and a Research Scientist position at the UPMC (2004-2008). Since 2008, she is an Associate Scientist (“Chargé de Recherche”) at the French National Centre for Scientific Research (CNRS) and currently with IMPMC-CNRS UMR 7590 at Sorbonne University in Paris, France. Her background is in signal and image processing for biomedical engineering applications such as functional electrical stimulation and computer-assisted surgery. Currently, she works in the area of methods development for the reconstruction of structure and dynamics of biological macromolecular complexes from cryo-electron microscopy images. She is particularly interested in the development of image analysis methods for studying continuous conformational changes of the complexes.
Susan studied medicine at the University of Oxford before undertaking a DPhil with Prof David Stuart using X-ray crystallography to determine the structure of foot and mouth disease viruses. She established her group with a Royal Society Dorothy Hodgkin Fellowship studying human viral-receptor interactions using both X-ray crystallography and electron microscopy. The work of the group gradually moved into work with bacterial pathogens and immune system components leading to her appointment as Chair of Microbiology in the Sir William Dunn School of Pathology, Oxford in 2006. Since 2016 she has been the first Scientific Director of the Central Oxford Structural Microscopy and Imaging Centre driving installation and user training in modern cryo-electron microscopy.
Rafael Fernandez Leiro is a Junior Group Leader at the Spanish National Cancer Research Center (CNIO).
He obtained his PhD in 2011 from the University of A Coruña in Spain where he worked in protein engineering using directed evolution techniques and structure-led rational design. During his PhD, he visited the Rocasolano Institute in Madrid where he was trained in X-ray crystallography. After obtaining the PhD, he joined the Lamers lab at the LMB in Cambridge to work on DNA repair and replication. The timing could not have been better as the cryo-EM “resolution revolution” was happening and the LMB was at the centre of it. For the next six years, he worked with Meindert Lamers and Sjors Scheres to study multiple DNA replication and repair complexes and understand how these systems are regulated using cryo-EM and biochemistry.
He has recently joined CNIO to lead the “Genome Integrity & Structural Biology” group that focuses on the study of the function and biological implications of macromolecular complexes responsible for the maintenance of the integrity of the genome and the role they play in disease.
Cindi Schwartz received her M.S. at the University of Texas, Arlington in 2001. She then worked as a staff scientist in the Boulder Lab for 3D Electron Microscopy of Cells at the University of Colorado under the direction of Dick McIntosh and later Andreas Hoenger until 2014. The Boulder Lab was an NIH Research Resource mandated to accomplish three things: 1) to improve tomography so that other electron microscopy labs could use the technology effectively, 2) to provide tomography services for those who did not have access to the technology, and 3) to disseminate tomography via various training mechanisms to the broader scientific community. In that way, she has been and continues to be an instructor at over 20 workshops and/or conferences where she has taught IMOD and/or SerialEM, the open-source software programs developed by David Mastronarde at the Boulder Lab. Presently, she is a staff scientist under the direction of Elizabeth Fischer at the National Institute of Allergy and Infectious Diseases, Rocky Mountain Laboratories location in Hamilton, Montana. There she continues her work on cryo-electron tomography as well as teaching IMOD and SerialEM. She is an avid supporter of open communication among the scientific community and believes that we can all learn from each other. Therefore she is passionate about teaching and learning from our up-and-coming young scientists who will continue to drive the momentum we currently have in 3D cryo-electron microscopy.
Henning Stahlberg studied Physics at the Technical University of Berlin, and obtained his PhD from the EPFL Lausanne in 2003 in Structural Biology (Groups Prof. Horst Vogel and Prof. Jacques Dubochet). He then obtained his Habilitation in the group of Prof. Andreas Engel at the Biozentrum of the University of Basel in 2008, and accepted in 2009 a faculty position in Molecular and Cell Biology at the University of California in Davis, CA, USA, where he established a laboratory for high-resolution structure determination of biological macromolecules by cryo-transmission electron microscopy. Since 2009, Stahlberg is Professor and director of the Center for Cellular Imaging and NanoAnalytics (C-CINA) of the Biozentrum at the University of Basel.
The Stahlberg group is focusing on Parkinson's Disease and on Membrane Protein Structures. The main method is cryo-electron microscopy, which is extended by multidisciplinary approaches, including use of neuronal cell cultures and human brain tissue, using expression and purification of relevant protein systems, and biophysical and structural investigations with a variety of tools.
We are also developing methods to advance imaging capabilities, ranging from microfluidic cell handling and proteome preparation, to developing instrumentation allowing the preparation of cryo-electron microscopy grids from nanoliters of sample (Braun team).
Dr. Volkmann's research focuses on the development and application of computational tools to bridge information between the atomic and cellular scales, covering more than six orders of magnitude from Ångstroms to tens of microns. Central to this effort is the analysis and interpretation of reconstructions from electron cryo-microscopy (cryo-EM) and cellular electron cryo-tomography (cryo-ET). During his education and career, he acquired a broad background in mathematics, physics, artificial intelligence research, structural and computational biology, and image processing. While at the Max-Planck Institute in Germany in the early 90’s, he carried out experimental and computational aspects of ribosome crystallography under the guidance of Prof. Ada Yonath who won the 2009 Nobel Prize in chemistry. As a postdoctoral fellow at the Keck Center, Brandeis University, Dr. Volkmann expanded his research to include cryo-EM, cryo-ET, and image analysis under the guidance of David DeRosier, one of the founding fathers of three-dimensional reconstruction and analysis techniques.
Dr. Peijun Zhang obtained her Ph.D. in Biophysics and Physiology from University Virginia, M.S. in Physics and B.S. in Electrical Engineering from Nanjing University, China. She was a postdoc and subsequently a staff scientist at the National Cancer Institute, NIH. In 2006, she joined the faculty of the University of Pittsburgh, and was promoted to associate professor with tenure in 2012. She recently joined the University of Oxford as a full professor, and jointly as the founding director of eBIC (the UK National Electron Bio-imaging Centre) at the Diamond Light Source. Her research focuses on the molecular mechanisms of large protein complexes and assemblies, in particular those involved in HIV-1 pathogenesis and bacterial chemotaxis signaling, by developing and combining novel technologies for high-resolution cryoEM and cryoET. She received many awards, including “Carnegie Science Emerging Female Scientist Award” (2014) and “Wellcome Trust Investigator Award” (2017).
Dr. Ludtke holds the Charles C. Bell Jr. Professorship of Structural Biology in the Department of Biochemistry and Molecular Biology at Baylor College of Medicine, where he directs the CryoEM Core and co-directs BCM's CIBR Center. His Ph.D. (Rice University) and BS (Caltech) are both in Physics, with a focus on molecular biophysics, which led to his development of the EMAN software suite for CryoEM image analysis in the late 1990s. He was awarded the Burton Medal by the MSA in 2008 for these developments. For the last 20+ years his group has focused on CryoEM, CryoET and novel image processing methods development, and EMAN remains one of the most widely used software packages in the field. In co-directing the National Center for Macromolecular for over 15 years, his group has developed biological interests spanning a wide range of systems, including chaperonins, ion channels, LDL/HDL, nuclear pore complexes and the structure of macromolecules within the cellular environment. Recent developments include applications of Deep Learning techniques to CryoEM and CryoET for particle selection and cellular tomography volume segmentation as well as applications of bispectral analysis to dramatically improve 2D image analysis and speed 3D structural refinements.
Maria Teresa Fernandez-Diaz is the Head of the Diffraction Group at the Institut Laue Langevin in Grenoble (ILL) which exploits eleven unique neutron diffractometers. She received her PhD in Solid State Physics at the University Autonoma of Madrid in 1991, followed by a postdoctoral fellowship at the Laboratoire Leon Brillouin in Saclay to develop a single-crystal neutron diffractometer for magnetic studies. In December 1994 she was appointed as Instrument Scientist at the ILL and acquired a large experience in neutron diffraction techniques in powder and single-crystal. Her scientific interest lays mainly in the field of strongly correlated electron systems and in particular the structural and magnetic aspects of oxides presenting charge, spin and orbital ordering phenomena. Progressively she has broadened her interests to different energy related materials as well as to magnetic ionic liquids, studying the correlation of their structural features with their relevant functional properties.
J. Manuel Perez-Mato is one of the founders and developers of the Bilbao
Crystallographic Server, a website with crystallographic programs freely
available on internet. After more than 30 years as Professor of Condensed
Matter Physics at the University of the Basque Country in Bilbao in Spain, he
has recently retired. His research interests include the characterization of phase
transitions and ferroic materials, and the development of advanced methods in
computational crystallography. His work has been especially intensive on the
application of the superspace formalism in the investigation of modulated and
modular structures. He has been member of the Executive Committee of the
IUCr, and of the editorial committees of several scientific journals. His most
recent activity has focused on the design of symmetry-based computational
tools for the analysis of magnetic structures.
Stefan Raunser was born 1976 in Landau in der Pfalz. He studied chemistry and biology at the Johannes-Gutenberg-Universität Mainz. He prepared his PhD thesis in the group of Werner Kühlbrandt at the Max Planck Institute of Biophysics in Frankfurt/Main and received his PhD in biochemistry at Johann-Wolfgang-Goethe Universität Frankfurt in 2004. From 2005 to 2008 he was a postdoctoral researcher in the group of Thomas Walz at Harvard Medical School in Boston, USA and from 2008 to 2013 he was Emmy Noether group leader at the Max Planck Institute of Molecular Physiology in Dortmund. From January to June 2014 he was Einstein-Professor for Membrane Biochemistry at Freie Universität Berlin. Since July 2014 he is Director and Scientific Member at the Max Planck Institute of Molecular Physiology in Dortmund.
Dorit Hanein is a Professor at the Sanford Burnham Prebys Medical Discovery Institute in La Jolla, California with adjunct appointments at University of California, San Diego and Institut Pasteur, France. Dr. Hanein received her Ph.D. in Chemistry from The Weizmann Institute, Israel, and pursued a Fulbright postdoctoral fellowship with Dr. David DeRosier at Brandeis University. Central to Hanein’s research is a critical question in cell biology: how do cells employ large, macromolecular machines in cellular processes. Dr. Hanein made seminal contributions to our knowledge of the cytoskeleton and its assemblies, to the development of cellular cryo-tomography of nanomachines in intact cells, and to the evolution of quantitative electron microscopy. Dr. Hanein is a leader in integrating imaging modalities across scales to permit the placement of molecular components of macromolecular complexes into their functional context in whole cells. Hanein’s lab continues to push the envelope in developing, and employing unique set of powerful tools, merging state of the art imaging technologies with sophisticated computational methods, mechanical engineering, cell biology, and protein biochemistry. The resulting quantitative integration of scales between macroscopic cellular behavior and high-resolution structural changes position these efforts at the front end of science with high impact in both medicine and basic biological research.
Branton J. Campbell earned an MA in physics and a PhD in materials science at the University of California at Santa Barbara and did post-doctoral research in the Materials Science Division at Argonne National Laboratory. He is now a Professor of Physics in the Department of Physics & Astronomy at Brigham Young University in the USA and a former Fulbright Scholar. His current research activities involve group-theoretical analysis of structural order parameters (atomic displacements, site occupancies, magnetic moments, lattice strains) arising from phase transitions, symmetry groups in commensurate and modulated crystals, and experimental x-ray and neutron-scattering studies of structure-property relationships in complex oxides. He is an active co-developer (with Harold Stokes) of the ISOTROPY Software Suite for the application of symmetry groups and representational analysis to solid-state phase transitions, including extensive support for magnetic structures. He currently serves as the vice-chair of the US National Committee on Crystallography and as the chair of the Commission on Magnetic Structure, which recently developed the magCIF standard for communicating magnetic-structure data.
IUCr Scientific Freedom Policy Statement. The Organizing Committee of “Magnetic Crystallography” Course of the International School of Crystallography shall observe the basic policy of nondiscrimination and affirms the rights of scientists throughout the world to adhere or to associate with international scientific activity without regard to such factors as ethnic origin, religion, citizenship, language, political stance, gender, sex or age, in accordance with the Statues of the International Council for Science. At this course no barriers will exist which would prevent the participation of bona fide scientists.
