Ettore Majorana Foundation and Centre for Scientific Culture
President: Professor Antonino Zichichi
Director: Sir Tom Blundell, FRS FMedSci
Over the last 50 years, crystallography has developed from a method capable of determining the structures of isolated, soluble proteins to one able to provide detailed information on mechanisms of action of integral membrane proteins, whole viruses and the complex nano-machines that are central to cellular function. To discover how biology works researchers are now combining the power of crystallography with multiple other methods, spanning from the atomic to cellular scale, and including revolutionary developments in electron cryo-microscopy and tomography. This Course will celebrate its milestone as the 50th in the crystallography series started by Dorothy Hodgkin by focusing on integration: 1) of different techniques, 2) of molecular and cellular approaches and 3) of the crystallographic community, including diversity.
The aim is to provide young researchers with a review of the fundamental approaches and latest developments in the application of crystallography and hybrid methods to the structure and function of biological macromolecules and complexes. Lectures will exemplify use of integrated approaches to analyse molecular mechanism in human and pathogen biology. There will be hands-on workshops to provide practical experience and in-depth discussion of topics ranging from sample preparation to data analysis software. To commemorate the achievements of the Erice crystallography school over the past 50 years, the course will feature several sessions that reflect on the past and look to the future to highlight the factors that create an inclusive discipline.
New for the 50th Erice School in 2017 is the Rising Star session featuring young crystallographers from around the globe speaking about their research.
Tick the box on the registration form if you're eligible for a Rising Star Award (current PhD student or PhD awarded after Dec 31 2013) and would like to be considered.
ETH, Zuerich, CH
Nenad Ban was born in Zagreb, Croatia and educated at the University of Zagreb. He continued with his studies in the US where he obtained a PhD degree at the University of California at Riverside in the group of Alexander McPherson. His interest in large macromolecular assemblies led him for his postdoctoral work to the Department of Molecular Biophysics and Biochemistry at Yale University where he determined the atomic structure of the large ribosomal subunit by X-ray crystallography, as part of the group in the laboratory of Thomas Steitz. These results demonstrated that the ribosome is a ribozyme.
Since 2000 Nenad Ban is a professor of structural molecular biology at the ETH Zurich. Structural studies in his group on bacterial and eukaryotic ribosomes and their functional complexes, using a combination of crystallographic, electron microscopic and biochemical experiments, have provided fundamental insights into the process of protein synthesis in all kingdoms of life. His group has obtained detailed structural information on eukaryotic ribosomes, which are at 4.3 MDa significantly larger and more complex than their 2.6 MDa bacterial counterparts, by determining the first complete structures of both eukaryotic ribosomal subunits each in complex with an initiation factor. Recently, his group also obtained a breakthrough in visualizing mammalian mitochondrial ribosomes with their high-resolution study that revealed its unusual structure and the mechanism of how mitochondrial ribosomes, specialized for the synthesis of membrane proteins, are attached to the membranes. Nenad Ban is a member of EMBO, the German Academy of Sciences, the Croatian Academy of Arts and Sciences and the recipient of several prizes and awards including the Heinrich Wieland prize, Roessler prize of the ETH Zurich, the Latsis prize, the Friedrich Miescher Prize of the Swiss Society for Biochemistry, Spiridon Brusina medal and the AAAS Newcomb Cleveland Prize.
LMB, Cambridge, UK
P. J. BJORKMAN
Caltec, Pasadena, US
Dr. Bjorkman received a B.A. degree in Chemistry from the University of Oregon and a Ph.D. degree in Biochemistry from Harvard University. As a graduate student and postdoctoral fellow in Don Wiley's laboratory, she solved the first crystal structure of a human histocompatibility complex molecule. She continued her postdoctoral training at Stanford with Mark Davis, where she worked on T cell receptors. She joined the faculty of Caltech in 1989. Dr. Bjorkman is a member of the US National Academy of Sciences, the American Academy of Arts and Sciences, the American Philosophical Society, and is a Fellow of the American Association for the Advancement of Science. She was the L'OREAL-UNESCO Women in Science North American Laureate (2006) and was named Among Most Powerful Moms in STEM (Science, Technology, Engineering, and Math) in Working Mother magazine (2011).
Dr. Bjorkman’s laboratory is interested in immune recognition of viral pathogens. We are particularly interested in understanding the immune response against HIV-1 and influenza in order to develop improved therapeutics. We use X-ray crystallography, electron microscopy, and biochemistry to study pathogen envelope glycoproteins and host immune response proteins. Using structural information and alternate antibody architectures, we are engineering antibody-based reagents with increased potency and breadth. We are also investigating the structural correlates of broad and potent antibody-mediated neutralization of HIV-1 to better understand what leads to naturally-occurring broad and potent antibodies. In related work, we use 3D imaging techniques such as electron tomography and fluorescent microscopy to investigate HIV/SIV infection in animal and human tissues.
Department of Biochemistry at Cambridge, UK
Tom Blundell maintains an active laboratory as Director of Research and Professor Emeritus in the Department of Biochemistry, University of Cambridge, where he was previously Sir William Dunn Professor and Head of Department between 1996 and 2009, and Chair of School of Biological Sciences between 2003 and 2009. He has previously held teaching and research positions in the Universities of London, Sussex and Oxford.
Tom continues to research on molecular, structural and computational biology of growth factors, receptor activation, signal transduction and DNA repair, important in cancer, tuberculosis and familial diseases. He has also published many widely used software packages for protein modelling and design including Modeller (8560 citations) and Fugue (1150 citations), as well as computer programs to predict the effects of mutations on protein stability and interactions (SDM & mCSM). Recently his group has produced computer programs (mCSM-lig) and databases to predict the affects of mutations on small-molecule binding, relevant to antibiotic resistance. He has published 560 research papers, including 30 in Nature and 20 in past year including two in Science.
Tom has developed new approaches to structure-guided and fragment-based drug discovery. In 1999 he co-founded Astex Therapeutics, an oncology company that has eight drugs in clinical trials and that was sold in 2013 as Astex Pharma to Otsuka for $886 million. In parallel in the University of Cambridge he has developed structure-guided fragment-based approaches to drug discovery for difficult targets involving multiprotein systems and protein-protein interactions for the Met receptor and DNA double-strand break repair Rad51-Brca2 complexes, based on his basic research programmes. He has also been targeting ~10 Mycobacterium tuberculosis proteins as part of the Gates HIT-TB and EU-FP7 MM4TB consortia, including structural and biochemical studies of resistance mutations to first line drugs.
Tom was a member of PM Margaret Thatcher’s Advisory Council on Science & Technology (1988-1990), founding CEO of Biotechnology and Biological Sciences Research Council, 1991-1996 (Chair 2009-2015), Chairman, Royal Commission on Environment (1998-2005), Deputy Chair of Institute of Cancer Research 2008-2015 and President of UK Science Council since 2011.
NYSBC, New York, US
Bridget Carragher received her Ph.D. in Biophysics from the University of Chicago in 1987. She then worked in a variety of positions, both in industry and academia until moving to the Scripps Research Institute in 2001. Since 2002 she has served as the Director of the National Resource for Automated Molecular Microscopy (NRAMM), an NIH funded national biotechnology research resource. The focus of NRAMM is the development of automated imaging techniques for solving three-dimensional structures of macromolecular complexes using cryo-transmission electron microscopy (cryoEM). The overall goal is to develop new methods to improve the entire process, from specimen preparation to the generation of the final three-dimensional map. In 2007 Bridget co-founded a new company, NanoImaging Services, Inc., whose goal is to provide cryoEM and other microscopy services to the biopharmaceutical and biotechnology industry. She serves as Chief Operations Officer of NanoImaging Services. In 2015 Bridget moved her academic lab from The Scripps Research Institute to the New York Structural Biology Center where she now serves as Co-Director of the Simons Electron Microscopy Center.
Baylor College of Medicine, Houston, TX, US
Wah Chiu received his BA in Physics (1969) and PhD in Biophysics (1975) from the University of California, Berkeley. He is the Alvin Romansky Professor of Biochemistry and the Director of the National Center for Macromolecular Imaging at Baylor College of Medicine in Houston, Texas. He is a pioneer in methodology development for electron cryo-microscopy. His work has made multiple transformational contributions in developing single particle electron cryo-microscopy as a tool for the structural determination of molecular machines at atomic resolution.
His research, collaboration and training activities in structural and computational biology have been recognized by his elected membership to the Academia Sinica, Taiwan (2008) and the United States National Academy of Sciences (2012) in addition to several honors including the Distinguished Science Award from the Microscopy Society of America (2014), Honorary Doctorate of Philosophy, University of Helsinki, Finland (2014) and the Barbara and Corbin J. Robertson Jr. Presidential Award for Excellence in Education, Baylor College of Medicine (2015).
MPI for Biochemistry, Munich, DE
Elena Conti studied chemistry at the University of Pavia in Italy and received her Ph.D. in 1996 from the Faculty of Physical Sciences at Imperial College in London. For her post-doctoral studies, Conti joined the laboratory of John Kuriyan at the Rockefeller University in New York, where she worked on the mechanisms of nuclear protein import. In 1999, she established her own research group at the European Molecular Biology Laboratory in Heidelberg. In 2007, Conti became Director and Scientific Member of the Max Planck Institute of Biochemistry in Munich, where she heads the department of Structural Cell Biology. Conti’s research is aimed at understanding how RNA export, surveillance and turnover are carried out by the concerted action of macromolecular machines using a combination of structural biology, biochemistry and biophysical approaches. In particular, her group has studied the mechanisms of mRNA surveillance centered at the exon junction complex and of RNA degradation by the exosome complex. In recognition of her work, Conti has been elected member of EMBO and of the Germany Academy of Science in 2009 and has been awarded several prizes, including the Leibniz Prize in 2008 and the Jeantet Prize for Medicine in 2014.
MRC, Cambridge, UK
I have studied molecular biology and structural biology at the University of Tuebingen, Technical University of Munich and Paul Scherrer Institute (CH). Following that, I started a PhD in the group of Prof. Henry Chapman at DESY in Hamburg (D). The main focus of my thesis was the development of the serial femtosecond crystallography approach at modern X-ray sources. Besides methodological developments, I was heavily involved in G-protein coupled receptor structural biology. In addition, I have adapted the serial crystallography approach to a synchrotron light source, which made this approach applicable to a wider community of structural biologists. In 2015, I graduated with summa cum laude in Chemistry at the University of Hamburg. After my PhD I was awarded with an HFSP long-term fellowship to join the laboratory of Dr. Sjors Scheres at the LMB, Cambridge (UK). The main focus of our group is methodological developments in the field of single particle cryoEM with a main focus on computational aspects.
Utrecht University, NL
Harvard University, Boston, US
Dr. Hur received her BS in physics from Ewha Women’s University in Korea in 2001, Ph.D. in physical chemistry with Dr. Thomas C. Bruice at the University of California, Santa Barbara in 2003, and post-doctoral training in X-ray crystallography with Dr. Robert M. Stroud at the University of California, San Francisco. Dr. Hur joined Harvard Medical School in 2008 as an assistant professor in Dept. of Biological Chemistry and Molecular Pharmacology. In 2014, she was promoted to an associate professor with a joint appointment at Boston Children’s Hospital. Dr. Hur is a recipient of the 2009 Massachusetts Life Sciences Young Investigator Award, the 2010 Pew Scholar Award, the 2015 Vilcek Prize for Creative Promise in Biomedical Science and the 2015 Burroughs Wellcome Infectious Disease Investigator Award.
Dr. Hur’s research focuses on structural and biochemical mechanisms of the immune system. Over the past several years, she and her research group have identified the mechanism by which the innate immune system distinguishes between self and non-self RNAs. In particular, the group has discovered the filamentous assembly architecture of the viral RNA sensors, MDA5 and RIG-I, and how the assembly structures and their dynamics are utilized for viral RNA detection and activation of the antiviral signaling pathway. More recently, Dr. Hur’s interest has expanded to a group of transcription factors that are involved in self vs. non-self discrimination in the adaptive immune system. These include AIRE and FOXP3 that play critical roles in eliminating or suppressing auto-reactive T cells.
MPI for Biophysics, Frankfurt, DE
Werner Kühlbrandt studied chemistry and crystallography at the Free University Berlin, and biochemistry and biophysics at King’s College London. He did his PhD with Nigel Unwin at the MRC Laboratory of Molecular Biology in Cambridge, UK, investigating the structure of two-dimensional ribosome crystals by electron microscopy. As a postdoc, he turned to structural studies of membrane proteins, first at the ETH Zürich, and then at Imperial College London, to determine the high-resolution structure of the plant light-harvesting complex, LHC-II. After a short stay at UC Berkeley, CA, he became a group leader at EMBL Heidelberg in 1988, where he solved the cryoEM structure of LHC-II at 3.4 Å resolution. Since 1997 he is a director at the Max Planck Institute of Biophysics in Frankfurt, Germany. His department of Structural Biology investigates the structure and function of membrane transport proteins by X-ray or electron crystallography, and the structure of large membrane protein complexes, such as the mitochondrial ATP synthase, by single-particle cryoEM and electron tomography.
Harvard University, Boston, US
Debora is a mathematician and computational biologist with a track record of using novel algorithms and statistics to successfully address unsolved biological problems. She has a passion for interpreting genetic variation in a way that impacts biomedical applications. During her PhD, she quantified the potential pan-genomic scope of microRNA targeting and combinatorial regulation of protein expression and co-discovered the first microRNA in a virus. As a postdoc she and her colleagues cracked the classic, unsolved problem of ab initio 3D structure prediction of proteins using a maximum entropy probability model for evolutionary sequences. She has developed this approach to determine functional interactions, biomolecular structures, including the 3D structure of RNA and RNA-protein complexes and the conformational ensembles of apparently disordered proteins. Her new lab at Harvard is now developing the algorithms to use in the quantitating the effects of genetic variants, including those involved in antibiotic resistance.
Max Planck Institute, Martinsried, DE
I received my bachelor degree in 1999 from University of Tokyo. In 2005, I received my PhD in biophysics (structural biology, cryo-EM) from University of Tokyo with a research that I conducted at University of Texas, Southwestern Medical Center under supervision of Prof. Masahide Kikkawa. Afterwards in 2007, I joined Alasdair Steven’s laboratory at National Institutes of Health as a research fellow. During my PhD and postdoc time, I have solved the structures of cytoskeleton microtubules bound to its motor protein dynein. Further, I proposed a mechanism for the assembly kinetics of the prion/amyloid protein HET-s by solving the HET-s amyloid structure at 8.5 Å, and I described membrane curvature formation by endocytotic proteins polymerizing on the surface of membranes. These experiences gave me a strong toolbox to follow dynamic protein assemblies and to understand their molecular mechanisms.
After I started my laboratory in 2012, I focused on elucidating fundamental questions how the change of the cell shape is governed and the involvement of the cytoskeleton in the processes. Since the start of my lab using cryo electron microscopes, we have been applying hybrid methods using in vitro reconstituted protein complexes. My laboratory is funded by research grants from the German Research Council (DFG) and the Boehringer Ingelheim Foundation for outstanding young group leaders. Since the start of the laboratory, we have published 12 papers including 3 papers with the correspondence. Since 2016, I am an EMBO Young Investigator.
Aarhus University, DK
Poul Nissen is Professor of Protein Biochemistry at the Department of Molecular Biology and Genetics at Aarhus University, director of the PUMPkin Centre of the Danish National Research Foundation, and director of the DANDRITE research institute, which is the Danish node of the Nordic-EMBL Partnership for Molecular Medicine. He is an elected member of EMBO and the Royal Danish Academy of Science and Letters and the Danish Academy of Technical Sciences.
Poul Nissen’s PhD (1994-1997) and postdoctoral (1997-2000) research focused on crystallographic studies of translation factors, tRNA and the 50S ribosome with PhD supervisor Jens Nyborg at Aarhus University and postdoctoral mentor (and later 2009 Nobel laureate) Tom Steitz at Yale University. Returning to Aarhus University to set up his own, independent research he put a main focus on the field of ion-pumping P-type ATPases, which was at that time highly developed at a biochemical point of view but as yet without detailed structural information.
His group has determined a large range of structures of P-type ATPases representing the full functional cycle of the sarco-endoplasmic reticulum Ca2+-ATPase (SERCA) and also several structures of the Na+,K+-ATPase. Furthermore, structures of plasma membrane Ca2+-ATPase and H+-ATPase and of bacterial Cu+ and Zn2+-ATPases have been determined in his lab. Besides P-type ATPases his lab also works on neurotransmitter and amino acid transporters of the SLC6 secondary transporter family. The lab uses a range of methods in biochemical and biophysical characterization and structural biology, primarily X-ray crystallography, electron microscopy, and small-angle scattering. He also actively pursues translational activties in drug discovery and biotech.
MRC, Cambridge, UK
I am originally from Canada and studied Biochemistry at the University of British Columbia in Vancouver. In 1999, I moved to the UK for PhD studies with David Barford at The Institute of Cancer Research. Here I studied the Anaphase Promoting Complex/Cyclosome (APC/C) by reconstituting its activity in vitro and studying its structure by electron microscopy. After completing my PhD, I moved to Cambridge where I was a Career Development Fellow at the MRC Laboratory of Molecular Biology in Venki Ramakrishnan’s lab, funded by a Beit Memorial Fellowship for Medical Research. In 2009, I started my own lab at MRC-LMB. I am also a fellow of Clare Hall. I was awarded an ERC Starting Grant in 2011 and was chosen to be an EMBO Young Investigator in 2015.
My work focuses on understanding the mechanisms of macromolecular protein complexes involved in regulating gene expression. I use an integrated approach combining structural, biochemical and functional studies. The lab aims to reconstitute multi-protein complexes and their activities, and determine their high-resolution structures to understand their mechanisms. Recent work has focused on the Cleavage and Polyadenylation Factor (CPF), the Pan2–Pan3 deadenylation complex and the Fanconi Anaemia core complex, an E3 ubiquitin ligase involved in DNA repair. My lab also recently developed new supports for electron cryo-microscopy (cryo-EM) that reduce radiation-induced specimen motion.
EMBL-EBI, Hinxton, UK
Ardan Patwardhan received his PhD from the Royal Institute of Technology (Sweden) in 1997 where his work involved the development of confocal microscopy systems. He later moved to Imperial College London where he focused mainly on methods development for single-particle EM. From 2011 onwards he has been leading the management and development of EM and cellular related resources and activities, including EMDB and EMPIAR archives, at PDBe, EMBL-EBI. Several new web services have been developed for searching, visualising, and validating EM structural data. Furthermore he has been involved in several major community wide efforts to drive the field forward. Current themes of his work include a) improving public archiving support for other bio-imaging modalities, b) improving the quality and content of the archived data and c) 3D volumetric searching of data in EMDB and PDB, and d) improved integration of cellular and molecular imaging data.
Institut Pasteur, Paris, FR
My research focuses on phenomena associated to polymers, proteins, and macromolecular complexes. I employ computational methods to study, analyze, simulate, and model processes related to biomolecules. I did my undergraduate studies in Physics at the University of Rome, with majors in statistical mechanics and soft-matter physics. I approached biophysics and biochemistry during my graduate studies at the University of Zurich, where I earned my PhD in 2008, and continued as a postdoc therein until 2010. During my postdoc in Andrej Sali's lab at University of California in San Francisco (2010-2014), I established my interest on the structural biology of large macromolecular complexes. At the end of 2014 I joined Michael Nilges research unit at Institut Pasteur, Paris, to continue my research on macromolecular modeling. Since October 2015, I am a permanent researcher at CNRS. During the last seven years I have been working on structural determination of macromolecular assemblies using integrative approaches. In particular, I focused on the structural interpretation and modeling of chemical cross-linking coupled with mass spectrometry (XL-MS) data, integrated with electron microscopy (EM) data and X-ray crystallography of protein domains. Furthermore, I have developed Bayesian inference methods that minimize the effects of data inconsistency during integrative modeling. This approach has a double benefit: first, data integration deals with the sparseness of individual datasets by considering several additive piece of information; second, the Bayesian approach guarantees an objective interpretation of the noise and ambiguity of the data, even when it was collected from an heterogeneous sample.
Purdue University, West Lafayette, US
I graduated from the University of London (B.Sc. (General), 1950; B.Sc. (Special), 1951; M.Sc., 1953) and the University of Glasgow (Ph.D., 1956), after which I was a postdoctoral fellow with Prof. William Lipscomb at the University of Minnesota at Minneapolis (1956-1958) and a Research Associate with Prof. Max Perutz at the MRC Laboratory of Molecular Biology, Cambridge, England (1958-1964). Currently I am the Hanley Distinguished Professor of Biological Sciences at Purdue University, where I have worked for the last 52 years. I am a member of the U.S. National Academy of Sciences, a foreign member of the British Royal Society, and a 2000-2006 member of the National Science Board, the oversight body for the National Science Foundation. I have received numerous international honors and have honorary degrees from universities in Canada, France, Sweden, England, and Belgium. My laboratory utilizes X-ray crystallography and electron microscopy to study the biological structure of various animal and bacterial viruses at atomic resolution to determine how these molecular assemblages recognize specific hosts, tissues, or cells; how they enter the cell and disassemble; and how newly synthesized viral components assemble and mature to form progeny viruses. I have studied single-stranded RNA rhino- (common cold), coxsackie-, polio-, and cardioviruses as well as the enveloped toga- and flaviviruses; single-stranded DNA human, canine, feline, and porcine parvoviruses and the bacterial φX174 virus; and the double-stranded DNA tailed φ29 and T4 bacteriophages.
The Rockefeller University, New York, US
I graduated from Cambridge University with a degree in Natural Sciences (Zoology), and then studied as a graduate student with John Kilmartin at the Laboratory for Molecular Biology in Cambridge, where for my Ph.D. project I developed techniques for the subfractionation of the yeast nucleus, isolating the yeast spindle organizer. We made a panel of monoclonal antibodies against these enriched fractions, eventually allowing the identification of yeast spindle pole and spindle-associated components and their subsequent functional characterization. We also showed that the complex structure of the yeast spindle organizer can be made simply from a few highly iterated proteins in successive crystalline layers. Then, as a postdoctoral researcher in Günter Blobel's laboratory at the Rockefeller University, I studied the NPC, which mediates trafficking between the cytoplasm and nucleoplasm, and also plays key roles in other crucial cellular processes. Using highly enriched yeast NPC fractions for a biochemical and structural approach, we generated the first inventories of its components. This work also demonstrated that there are distinct transport pathways, with many different but partially redundant and overlapping transport pathways all converging at the NPC.
In 1997 I started my own laboratory at the Rockefeller University, the main focus of which remains the NPC. Our studies have led to the first maps of the three-dimensional architecture of the NPC and the position of all its components, revealing the common evolutionary origins of this structure with vesicle coating proteins, and suggesting a model explaining the overall transport mechanism. We ultimately aim to generate dynamic maps of the transporting NPC at the atomic and microsecond level of resolution. We have also studied the kinetics of transport, revealing roles for binding and competition in the mechanism of the NPC, and how multiple and extremely rapid interactions between cargo-carrying transport factors and proteins in the NPC mediate both fast and specific nuclear trafficking.
Our NPC studies are examples of the potential of the our proteomic, structural and computational approaches, that have allowed us to dissect the structure and function of diverse macromolecular assemblies and interactome networks. Hence, in 2005, we formed the National Center for Dynamic Interactome Research (NCDIR; http://www.ncdir.org/). The central goal of the NCDIR is to address the urgent need for technologies that can rapidly, reliably, and routinely reveal and interpret the dynamic cellular interactome. These technologies are designed to enable the community to assemble detailed, dynamic representations of the interactions in the cell.
Harvard University, Boston, US
Chris Sander is theoretical physicist turned computational biologist. The field of computational biology, which he helped develop, aims to solve important problems in biology using techniques of mathematics, physics, engineering, and computer science. Sander's current research is in computational genomics, protein structure and function, and systems pharmacology to help cure cancer. He developed perturbation biology, a method used to compute response to combinatorial therapy aiming to block the emergence of resistance to otherwise successful targeted cancer therapies. With Niki Schultz and Ethan Cerami as information resource architects, he led the creation of the cBioPortal for Cancer Genomics (cbioportal.org). With Debora Marks and colleagues, in 2010, he brought the previously unsolved problem of 3D fold prediction to an effective and practicable solution using statistical physics and information from evolutionary sequence information (EVfold.org). Currently in Boston, Sander is director of the cBio Center at Dana-Farber Cancer Institute focussed on computational and systems biology and Professor of Cell Biology at Harvard Medical School. Earlier, he was founding director of the Computational Biology Center at Memorial Sloan Kettering Cancer Center and Tri-Institutional Professor at Rockefeller and Cornell Universities; Chief Information Science Officer at Millennium Pharmaceuticals, co-founder of the research section of the European Bioinformatics Institute and founding chair of the department of Biocomputing at the European Molecular Biology Laboratory in Heidelberg. As postdoc, he worked with Shneior Lifson at the Weizmann Institute in Rehovot and with Georg Schulz and Ken Holmes at the Max Planck Institute for Biophysics in Heidelberg. His Ph.D. is in theoretical physics.
Merck, Kenilworth, US
I graduated Magna cum Laude in 1985 from Padova University (Italy) with a degree in Organic Chemistry. In 1989 I received my PhD in Organic Chemistry from the same university with a thesis in Structural Biology. In February 1990 I joined the laboratory of Dr. James C. Sacchettini at the Albert Einstein College of Medicine, Bronx (NY), as postdoctoral fellow, and subsequently as Instructor. My interest was initially for a class of small fatty acid binding proteins that had been related to obesity and diabetes. Subsequently most of my work was involved in bacterial enzymes that could be used as target for the design of novel antibiotics. During the 6 years I spent there, I mentored several graduated students and post-doctoral fellows.
In 1997 I joined Merck and Co., Inc, where I was involved in several projects, providing structural biology support for diabetes, inflammation and oncology targets. I developed and still maintain a particular interest in the structural aspects of Protein Kinases inhibition. My more recent work focused on the diabetes target DPP-4, and on how structural biology and modeling have helped the development of several potent inhibitors, and on the structure-function of antibodies. I published over 70 papers in peer-reviewed journals, and I have been invited to give several talks about my research at local universities and national and international meetings.
Heidelberg University, DE
I graduated in 1984 from the Ludwig-Maximilian University in Munich with the state exam in food chemistry. Despite this “exotic” start, I received my PhD in Biochemistry in 1989 from the same university for my thesis in biochemistry on the photosynthetic reaction center with H. Michel at the Max-Plank-Institute (MPI) in Martinsried. I followed him as a post-doctoral fellow to the MPI of Biophysics in Frankfurt, and in 1991 I joined Prof. Alwyn Jones at the Biomedical Center in Uppsala (Sweden) where I continued my training in protein crystallography working on various enzymes. In 1994 I became an independent group leader in the Structural Biology Programme at the EMBL in Heidelberg. During this time, I got interested in membrane protein biogenesis and protein targeting. Since 2000 I am full professor at Heidelberg University teaching biochemistry and structural biology, and I have supervised more than 50 graduate students and postdocs. Since I started my independent career, the signal recognition particle and related targeting systems became one of my main interests. More recent work also includes ribosome biogenesis and ribosome associated factors, which act early on the nascent chain and comprise targeting factors, enzymes and chaperones. A particular interest of my group are RNA-protein complexes and the combination of hybrid approaches in order to obtain mechanistic insights into the proteins, complexes and pathways of our interest.
NKI, Amsterdam, NL
University of Oxford, UK
After a first degree in biophysics at King’s College London, I learnt protein crystallography at Bristol University during a PhD. I then moved to Oxford, and have been there mainly since, the largest interruption being a period spent working in China from 1981-83, at the Institute of Biophysics, Beijing. I am now an MRC research professor in the Division of Structural Biology, where my group has a major focus on structural virology, including structural analyses of viruses and virus-cell interactions to understand the fundamental biology of viruses and how this might be used to facilitate the development of new therapies, including antivirals and structure-based vaccines. Current work increasingly uses advanced cryo-electron microscopy to study both the viruses and their interaction with cells in molecular and atomic detail.
In addition to the fundamental biomedical research I have a longstanding interest in technology and infrastructure development. For example establishing the Oxford Protein Production Facility, and coordinating the pan European activities in biomedically-led structural proteomics (SPINE and SPINE-II Complexes). Currently I am director of Instruct, a pan European Infrastructure for Integrated Structural Biology. In addition I helped establish the UK National Centre for biological Electron Microscopy (eBIC), the first such user facility embedded at a synchrotron source. For some years I have also led life science developments at Diamond Light Source – a leading synchrotron for macromolecular structure determination.
NCI, Bethesda, US
Dr. Subramaniam received his Ph.D. in Physical Chemistry from Stanford University and completed postdoctoral training in the Departments of Chemistry and Biology at M.I.T. He is a currently a Senior Investigator at the NIH, and the founding Director of both the Center for Molecular Microscopy, and the National Cryo-EM Laboratory at the National Cancer Institute, NIH. He also holds visiting faculty appointments at the Johns Hopkins University School of Medicine and University of Maryland, College Park. His current work is focused on the development of advanced technologies for imaging macromolecular assemblies using 3D electron microscopy, and their application to address fundamental problems in HIV/AIDS, metabolism and cancer research.
ICR, London, UK
Dr Alessandro Vannini studied Biology at the University of Rome "Roma Tre" and undertook his Ph.D. research at IRBM "P. Angeletti" (Merck Research Lab), Rome, focussing on the structural characterisation of quorum-sensing proteins in pathogenic bacteria and of human histone-deacetylases (HDACs). For his post-doctoral research, supported by Marie-Curie and EMBO long-term fellowships, he joined Professor Patrick Cramer's laboratory in Munich, focussing on the architecture and regulation of yeast RNA polymerase III, the largest among the three eukaryotic RNA polymerases, by combining X-ray crystallography and cryo-electron microscopy. In 2012, Dr Alessandro Vannini joined the Institute of Cancer Research in London, UK, as Team Leader in the Division of Structural Biology. Using an Integrative Structural Biology approach, he and his team are focusing on the structural and functional characterisation of large macromolecular complexes that assemble at RNA polymerase III binding sites across the eukaryotic genome, in order to understand their role in tumorigenesis as well as in the 3D spatial organization of the genome. In 2016, Dr. Vannini was elected EMBO Young Investigator and Wellcome Trust Investigator.
A. van OIJEN
University of Wollongong, AU
After receiving his PhD in Physics from Leiden University (the Netherlands) in 2001, Antoine van Oijen was a postdoctoral fellow in the group of Sunney Xie at Harvard University’s Chemistry department. In 2004, he started his own group at Harvard Medical School, followed by a move back to the Netherlands in 2010 as a full professor at Groningen University. In 2015, he moved to the University of Wollongong, Australia, as an Australian Research Council Laureate Fellow.
His research centers on the development and use of single-molecule biophysical tools to study complex biochemical systems. In particular, he is interested in understanding the mechanistic principles underlying the process of DNA replication. Using novel single-molecule fluorescence imaging and mechanical manipulation techniques, his work has allowed the direct visualization of the dynamics of individual replication complexes and has led to new insights into how genomic DNA is copied before cell division.
NIDDK, Bethesda, US
I have been a principal investigator in the Laboratory of Molecular Biology of the National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, since 1995. I was born in Shanghai, China and is a naturalized US citizen. I began her undergraduate studies of biochemistry at Fudan University in Shanghai before transferring to SUNY at Stony Brook to complete a B.A. degree. I received my Ph.D. in Biochemistry and Molecular Biophysics from Columbia University and held postdoctoral fellowships both at Columbia and Yale Universities. In 2011 I received the Dorothy Crowfoot Hodgkin Award from the Protein Society. I have been a elected member of the National Academy of Sciences (NAS) since 2013 and the American Academy of Arts and Sciences (AAAS) since 2015.
My current research centers on understanding the molecular mechanisms of DNA replication, repair and recombination with a focus on translesion DNA synthesis, genetic rearrangement and mismatch and nucleotide excision repair of damaged DNA. My group employs a multifaceted approach for analyzing the structures and activities of protein and nucleic acid molecules, including X-ray crystallography, electron microscopy, molecular biology, enzymology, and protein and nucleic acid chemistry. We have shown how different repair processes and directional motions are coupled to the energy supply of the cell, and how lesions in DNA can be avoided and bypassed by specialized synthetic enzymes. We have described how the substrate specificity of many enzymes is determined by a stringent requirement for a pair of metal ions held in a particular conformation. Recently our team has made use of crystallographic techniques to obtain the first atomic-resolution and time-resolved picture of DNA synthesis, discovering transiently associated metal ions that are essential for the addition of each new nucleotide unit.
Imperial College London, UK
Xiaodong Zhang graduated from Peking University in 1988, studying Nuclear Physics. She then continued her study in the United States and went to Stony Brook University to pursue her PhD in physics in the group of Professor Janos Kirz and David Sayre developing X-ray microscopy with chemical contrast. After she obtained her PhD in 1995, she decided to switch to biophysics/structural biology and went to Harvard University for her postdoctoral training under the guidance of Professor Don Wiley. She went to London, England in 1997 as a postdoctoral researcher at Imperial Cancer Research Fund (now part of Francis Crick Institute). She became a lecturer at Imperial College London in 2001, promoted to Reader in 2005 and became a Professor of Macromolecular Structure and Function in 2008. She is also a visiting professor of Peking University School of Life Sciences since 2007. Her current research focuses on using advanced structural biology and biophysical techniques such as x-ray crystallography and electron microscopy to study the macromolecular complexes inside our cells, especially those involved in gene regulation and DNA damage response. She aims to obtain movies of these complexes in action at the atomic level that will ultimately lead to a deeper understanding of the working these machines and novel therapeutic approaches for cancer and other human diseases.