Project Evaluation Committee (PEC) members

Name, Institution, Country Role
Joel L. Sussman, The Weizmann Institute of Science, Israel Panel Chair
Guillermo Montoya, Centro Nacional de Investigaciones Oncologicas (CNIO), Spain Panel Member
Keith S. Wilson, University of York, United Kingdom Panel Member
Giuseppe Zanotti, University of Padua, Italy Panel Member
Yves Muller, University of Erlangen, Germany Panel Member
Petr Leiman, Ecole Polytechnique Federale de Lausanne (EPFL), Switzerland Panel Member
William (Bill) Hunter, Dundee University, United Kingdom Panel Member
Catherine Birck, IGBMC, France Panel Member
Anastassis Perrakis, The Netherlands Cancer Institute (NKI), Netherlands Deputy Panel Chair
Ignacio Fita, Institute for Research in Biomedicine (IRB), Spain Panel Member
Michael Elbaum, The Weizmann Institute of Science, Israel Panel Member
Patrice Vachette, IBBMC, Universite Paris-Sud, France Panel Member
Kristina Djinovic-Carugo, University of Vienna, Austria Panel Member
Mirjam Czjzek, CNRS, France Panel Member


Joel L. Sussman

Prof. Joel L. Sussman is the Morton and Gladys Pickman Professor of Structural Biology at the Weizmann Institute of Science, and the Director of the Israel Structural Proteomics Center (ISPC, He is a member of the European Molecular Biology Organization (EMBO) and the Executive Board, International Structural Genomics Org (ISGO) and on the editorial board of Proteins, PEDS & PLoS ONE. He is an Honorary Professor of the Chinese Academy of Sciences, received the Bergmann Prize for Outstanding Research in Chemistry in Israel (1979), the U.S. Army Science Conference Award for Outstanding Research (1991), the Elkeles Prize for Outstanding Scientist in Medicine in Israel (2005), the Teva Founders Prize for Breakthroughs in Molecular Medicine (2006) and. From 1994 -1999 he was the director of the Brookhaven Protein Data Bank (PDB). He obtained his B.A. at Cornell University in 1965, and his Ph.D. in biophysics at MIT in 1972. His research group, at the Weizmann Institute, is studying the 3D structure/function of nervous system proteins, including β-secretase, acetylcholinesterase, cholinesterase-like adhesion molecules (CLAMs), β-glucosidase (the enzyme that is defective in Gaucher disease) and paraoxonase (a key enzyme that helps rid the arteries of plaque-forming clumps of LDL (“bad” cholesterol) that can lead to arteriosclerosis). The goal of his research is to use the 3D structures of proteins that his group is determining as a basis for new leads for treating neurological disorders, such as Alzheimer's Disease, autism, and in developing new therapies for Gaucher and arteriosclerosis. He is also studying intrinsically flexible (disordered) proteins. Most recently he and his colleagues have developed Proteopedia, the free, collaborative 3D encyclopedia of proteins & other molecules (

Guillermo Montoya

Guillermo Montoya began his scientific career in macromolecular membrane protein complexes at the Spanish National Research Council (CSIC), and got his degree from the University of Zaragoza. He moved in 1993 to the Max Planck-Institut für Biophysik in Frankfurt am Main and in 1994 he moved to EMBL-Heidelberg after obtaining an EMBO and Marie Curie EU postdoctoral fellowships where he pioneered the study of the structure of the signal recognition particle. In 2002 he was appointed as Group Leader at the Spanish National Cancer Research Centre (CNIO). Since them his work has been focused in the study of protein-protein and protein-DNA complexes, setting the basis to redesign their DNA binding specificity, thus generating tools that can be used to correct mutations. His main interests also include the molecular understanding of the role played by macromolecular complexes involved in oncogenic processes.

Keith S. Wilson


Giuseppe Zanotti

Giuseppe Zanotti graduated in chemistry in Padua in 1974 and he is now Full Professor of Biochemistry at the same University. Since the beginning of its scientific career he has worked at the determination of the structure of molecules and macromolecules through x-ray diffraction. After a Dr degreedissertation on bovine pancreatic Ribonuclease, he has solved the structure of small molecules till the end of the ’70. In 1979-80 he has spent one year at the Laboratory of Molecular Biophysics in Oxford, working with Louise Johnson on the structure of glycogen phosphorylase b. Back to Padua, he has been interested in proteins that bind and transport small hydrophobic molecules, in the structural determination of protein kinase CK2/inhibitor complexes and, more recently, in that of proteins from pathogenic bacteria, in particular H. pylori. He has also been interested in theoretical aspects of the phase problem and on the analysis and conformational aspects of the structure of globular proteins.

Yves Muller

Yves Muller studied chemistry in Freiburg (Germany). After completing his Ph.D. thesis with Prof. Georg Schulz in Freiburg in 1993, two postdoctoral stays at Genentech., Inc. (San Francisco) and Max-Delbrück-Center for Molecular Medicine (Berlin), he became a Reader in Biochemistry at University of Sussex (Brighton, UK) in 2001 and a Professor in Biotechnology at University Erlangen-Nuremberg in 2003 (Erlangen, Germany). His research expertise covers structure-function relationships in bacterial transcription regulators and blood hormone-binding globulins using a variety of molecular biology, biochemistry, X-ray crystallography and computational protein design tools.

Petr Leiman

Petr Leiman is a graduate of Moscow Institute of Physics and Technology. He received his Ph. D. and did postdoctoral training with Michael Rossmann at Purdue University. From 2008 he is an Assistant Professor of Biophysics and Head of the Laboratory of Structural Biology and Biophysics at École Polytechnique Fédérale de Lausanne (Swiss Institute of Technology in Lausanne). Petr Leiman is an expert in macromolecular crystallography and cryo-electron microscopy. His research interests are the structure and function of large macromolecular machines such as bacteriophages with contractile tails, R-type pyocins and the bacterial type VI secretion system.

William (Bill) Hunter

William (Bill) Hunter completed a PhD at the University of Glasgow, then post-doctoral research at the Universities of Sydney and Cambridge. He was staff member in the Department of Chemistry at the University of Manchester from 1989 to 1996, when he moved to the University of Dundee. He held several prestigious fellowships including for 10-yrs a Wellcome Trust Senior Fellowship. His research, in the area of structural enzymology, seeks to understand the chemical biology of complex biosynthetic processes and where appropriate to exploit the knowledge to support early stage drug discovery targeting neglected diseases. He has over 25-yrs experience with crystal structure determination and functional characterization of macromolecules, in excess of 150 Protein Data Bank entries with over 170 publications and is a Fellow of the Royal Society of Chemistry, the Royal Society of Edinburgh and the Academy of Medical Sciences.

Catherine Birck

Catherine Birck obtained her doctor of Pharmacy diploma in 1992. She did her doctoral research at the Institute of Pharmacology and Structural Biology and received her PhD from the University of Toulouse III in 1995. After three years as a post-doctoral fellow, she obtained a CNRS position and worked as staff scientist on structural studies of signal transduction protein complexes. She has extensive experience in protein production, crystallization, biophysical characterization including small-angle X-ray scattering studies, diffraction data collection and macromolecular X-ray crystallography studies. Since 2010, she is the head of Structural Biology and Genomics Technology Platform at CEBGS-IGBMC (Strasbourg). Her current research interests are shared between structural biology projects (structure function relationships of macromolecular complexes involved in transcription and epigenetic regulation) and methods development for protein production and biophysical characterization of macromolecular complexes.

Anastassis Perrakis

Anastassis (Tassos) Perrakis did his doctoral research at the European Molecular Biology Laboratory (EMBL) Hamburg unit, and received his PhD from the University of York in 1996. After two years as an EMBO post-doctoral fellow, he was appointed as staff scientist at the EMBL-Grenoble outstation. From 2000 he is a group leader at the Netherlands Cancer Institute. Dr. Perrakis has been involved in methods development for protein production, crystallization and diffraction data collection for macromolecular X-ray crystallography, and he is a keen user of small angle X-ray scattering. His current research interests are shared between structural biology (structure function relationship of proteins regulating mitosis and DNA replication, and inhibitor design for cancer targets) and methods development for macromolecular X-ray crystallography (ARP/wARP, PDB_REDO).

Ignacio Fita


Patrice Vachette

Patrice Vachette received his PhD from the University of Strasbourg in 1979. After two years as an EMBO post-doctoral fellow at the EMBL in Heidelberg, he was appointed as a CNRS staff scientist  at the French synchrotron radiation facility LURE in Orsay. He was in charge of the SAXS instrument and of applications of SAXS to biology. In 2004, after LURE shutdown, he moved to the IBBMC (Orsay) where his group is involved in numerous projects centered around the use of SAXS to study a great variety of biological systems.

Michael Elbaum

Michael Elbaum received his PhD in physics in 1991 from the University of Washington, where he studied the melting of (water) ice by optical methods. Since 1995 he is a faculty member in the Materials and Interfaces Department at the Weizmann Institute of Science. His research interests focus on physics of biological materials and cellular sub-systems. He has worked on elastic properties of cytoskeletal filaments, anomalous diffusion in the cell, and macromolecular exchange between the nucleus and cytoplasm. His work exploits a wide variety of experimental methodologies, centering on optical and electron imaging. Since 2006 he has been actively involved in soft X-ray imaging and cryo-tomography at BESSY II.

Kristina Djinovic-Carugo

Kristina Djinović-Carugo graduated in Chemistry at the University of Ljubljana. She did her doctoral research at the University of Pavia and received her PhD degree from University of Ljubljana in 1992.  She subsequently stayed as a post-doctoral fellow in the University of Pavia for three years. In 1995 she moved as an EMBO post-doctoral fellow to EMBL-Heidelberg, where she joined the group of Matti Saraste. After two years she was appointed a staff scientist to Structural and Computational Biology Programme at EMBL-HD. In 1999 she joined Sincrotrone Trieste – Elettra, as head of Structural Biology Laboratory, and subsequently as Head of Crystallography and Structural Biology Unit. In 2004 she was appointed full professor in Molecular Structural Biology at University of Vienna where she has been since. As of 2009 she serves as Head of Department for Structural and Computational Biology, and since 2010 as director of Center for Optimized Structural Studies. She has experience in protein production, crystallisation, biophysical characterisation, and over 25 years stage in X-ray crystallography. In perusing her main research focus – structural studies of the protein-protein interaction network in the striated muscle Z-disk, she is combining high resolution studies (X-ray diffraction, NMR), with complementary lower resolution techniques - small angle X-ray scattering, electron microscopy as well as distance sensitive spectroscopic methods as targeted spin-label EPR and chemical cross-linking combined with mass-spectroscopy. The goal of this research is to contribute to generation of structural picture of macromolecular assemblies at Z-disk and, together with cell-biology studies, to understanding its function and regulation at molecular level. She also has keen interests in methodological questions centred on X-ray induced radiation damage and use of soft X-rays in macromolecular crystallography.

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