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Ettore Majorana Foundation and Centre for Scientific Culture
President: Professor Antonino Zichichi

INTERNATIONAL SCHOOL of CRYSTALLOGRAPHY

Director: Sir Tom Blundell, FRS FMedSci

Erice, Italy • 2 June (arrival) to 11 June (departure) 2017

Course Directors

E. Yvonne Jones

University of Oxford, UK

Jennifer L. Martin

Griffith University
Brisbane, AU

Jennifer L Martin

Professor Jennifer L Martin is the newly appointed Director of the Eskitis Institute at Griffith University in Australia. Jenny trained as a pharmacist in Melbourne, Australia, and was the Gold Medallist of her year at the Victorian College of Pharmacy. She was subsequently awarded a Royal Commission for the Exhibition of 1851 Science Research Scholarship to undertake a DPhil research degree at the University of Oxford, in protein crystallography and structure-based inhibitor design. She established her own lab at the University of Queensland just 3 years after her PhD was awarded, in the Centre for Drug Design and Development, with a move 10 years later to the Institute for Molecular Bioscience. Her research focuses on protein structure and function in health and disease and the application of structure-based approaches to develop new drugs. Jenny is Vice-President of the Asian Crystallography Association, a former President of the Society of Crystallographers in Australia and New Zealand, and a former chair of the National Committee for Crystallography of the Australian Academy of Science. She is a strong advocate for gender equity, a member of the Australian NHMRC Women in Health Science Committee, and a founding member of the Science in Australia Gender Equity (SAGE) Steering Committee for the Academy of Science. SAGE recently launched an Australian pilot of the UK Athena SWAN awards program for gender equity in STEMM. Jenny is the recipient of many awards including an inaugural ARC Australian Laureate Fellowship, the ASBMB Roche Medal, the Queensland Smart Women Smart State Research Scientist Award, and the Women in Biotech Outstanding Achievement Award.

New for 2017

Rising Star Session

more info
Apply now!

Application deadline

30 November 2016

Purpose of the course

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.

Rising Star Session

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.


Speakers

click on the name to see bio-sketches
 

N. BAN
ETH, Zuerich, CH

 

D. BARFORD
LMB, Cambridge, UK

P. J. BJORKMAN
Caltec, Pasadena, US

Pamela J. Bjorkman

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.

B. CARRAGHER
NYSBC, New York, US

Bridget Carragher

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.

W. CHIU
Baylor College of Medicine, Houston, TX, US

Wah Chiu

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).

E. CONTI
MPI for Biochemistry, Munich, DE

Elena Conti

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.

C. GATI
MRC, Cambridge, UK

Cornelius Gati

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.

 

P. GROS
Utrecht University, NL

S. HUR
Harvard University, Boston, US

Sun Hur

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.

W. KÜHLBRANDT
MPI for Biophysics, Frankfurt, DE

Werner Kühlbrandt

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.

J. KURIYAN
University of California at Berkeley, US

John Kuriyan

Dr. Kuriyan earned his PhD in 1986 from the Massachusetts Institute of Technology. He was a post-doctoral fellow with Professors Martin Karplus (Harvard) and Gregory A. Petsko (MIT). From 1987 to 2001 he was on the faculty of The Rockefeller University, New York, where he was promoted to full Professor in 1993. He is a Professor of Molecular and Cell Biology and also of Chemistry at the University of California, Berkeley, a position he has held since 2001. Dr. Kuriyan is also an investigator of the Howard Hughes Medical Institute, having been appointed in 1990.
Dr. Kuriyan's research concerns the atomic-level structure and mechanism of the enzymes and molecular switches that carry out cellular signal transduction. His laboratory uses x-ray crystallography to determine the three-dimensional structures of proteins involved in signaling, as well as biochemical, biophysical, and cell biological analyses to elucidate mechanisms. Breakthroughs from the lab have included determining the auto-inhibited structures of several tyrosine kinases, including Src family kinases and elucidating the mechanism of allosteric activation of the kinase domains of the EGF receptor. His laboratory has provided a fundamental understanding of the structure and regulation several other signaling proteins, including STATs, the Ras activator SOS, and calcium/calmodulin-dependent protein kinase-II. Their structural insights have helped understand how the misregulation of these enzymes is often coupled to cancer and immune diseases and has implications for the development of kinase-targeted drugs to treat these diseases. His lab has also made fundamental contributions to understanding the structural basis for high-speed DNA replication. Dr. Kuriyan’s achievements in science have been recognized by numerous honors:
Foreign Member of The Royal Society, London. Elected April 2015.
Doctor of Humane Letters, honoris causa, Juniata College, Huntington, PA. May 2014. Merck Award, American Society of Biochemistry and Molecular Biology, 2009.
Fellow, American Academy of Arts and Sciences, Elected 2008.
Richard Lounsbery Award, US National Academy of Sciences, 2005.
Member, US National Academy of Sciences, Elected 2001.
Cornelius Rhoads Memorial Award, American Association for Cancer Research, 1999. Eli Lilly Award of the American Chemical Society, 1998.
DuPont-Merck Award of the Protein Society, 1997.
Schering-Plough Award of the American Society of Biochemistry and Molecular Biology, 1994.
Pew Scholar in the Biomedical Sciences, 1989-1993.

D. MARKS
Harvard University, Boston, US

Debora S. Marks

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.

 

N. MIZUMO
Max Planck Institute, Martinsried, DE

P. NISSEN
Aarhus University, DK

 

L. PASSMORE
MRC, Cambridge, UK

Lori Passmore

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.

M. ROSSMANN
Purdue University, West Lafayette, US

Michael G. Rossmann

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.

M.P. ROUT
The Rockefeller University, New York, US

Michael P. Rout

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.

G. SCAPIN
Merck, Kenilworth, US

Giovanna Scapin

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.

I. SINNING
Heidelberg University, DE

Irmgard Sinning

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.

T. SIXMA
NKI, Amsterdam, NL

 

D.I. STUART
University of Oxford, UK

David I. Stuart

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.

S. SUBRAMANIAM
NCI, Bethesda, US

Sriram Subramaniam

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.

A. VANNINI
ICR, London, UK

Alessandro Vannini

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

Antoine van Oijen

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.

W. YANG
NIDDK, Bethesda, US

Wei Yang

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.

X. ZHANG
Imperial College London, UK

Xiaodong Zhang

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.


Previous Schools

2016 • 49th Course
High-pressure crystallography: status artis and emerging opportunities
Directors: Francesca P.A. Fabbiani · John B. Parise · Malcolm Guthrie

2015 • 48th Course
Engineering Crystallography: from Molecule to Crystal to Functional Form
Directors: Kevin Roberts · Rui Tamura · Robert Docherty

2014 • 47th Course
Structural Basis of Pharmacology: Deeper Understanding of Drug Discovery through Crystallography
Directors: Eddy Arnold · Robert Stroud · Richard Pauptit · Giovanna Scapin

Future Schools

2018 • 51st Course
Electron Crystallography

2018 • 52nd Course
Quantum Crystallography

2019 • 53rd Course
Magnetic Crystallography

2019 • 54th Course
Electron Microscopy