Executive Committee and Council News
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The European Crystallographic Association has awarded the third Max Perutz Prize to
The third Max Perutz Prize of the European Crystallographic Association for 2007 is awarded to Prof. David Stuart in recognition of his impact in the field of virus crystallography. Prof Stuart is based at The Wellcome Trust Centre for Human Genetics in Oxford, UK
His research on virus structure, assembly and interactions with receptors not only includes detailed work on some of the most complex and relevant macromolecular assemblies currently amenable to crystallographic study, but also aims at developing vaccines and treatments of diseases.
He performed exceptional experiments in determining the largest crystal structures ever solved: viruses of 100Mda. His work is extensive and he has published more than one hundred papers in the past decade, seven of them in Nature and six in PNAS. Eight of these papers have been cited more than 100 times.
In summary, David Stuart is one of the pioneers of virus crystallography in the world and the ECA Prize 2007 is in recognition of his impact in this field, and his contributions to the structural chemistry of disease at the atomic level.
The European Crystallographic Association has awarded the second Max Perutz Prize to
for developing, implementing, teaching and applying the best tools available to produce macromolecular structures of highest quality.
Eleanor Dodson is an unusual scientist who has made unusual and remarkable contributions. Since the early years of working on insulin together with Prof. Dorothy Hodgkin, she has been at the center of the mathematical side of macromolecular crystallography and has been developing, implementing, teaching and applying the best tools available to produce science of highest quality.
Protein crystallography is a science that requires skills from many disciplines. The areas range from cell biology over DNA technology and the means to express exotic proteins in large quantities to statistical and mathematical methods to achieve optimal diffraction measurements and phase angle determinations with different methods and to validate the determined structures. Eleanor Dodson has throughout her career been engaged in the methodology in macromolecular crystallography, developing, implementing and applying mathematical and statistical methods for data collection and phasing (molecular replacement), refinement (maximum likelihood refinement of protein structure), and structure validation. This is only partly evident from her publication record. However, she has an extensive list of publications (close to 60 publications in the period 1995-2004), many of them in highly prestigious journals with outstanding number of citations (one method-paper received ~2100) showing the high impact and practical importance of her research.
Eleanor Dodson is also recognised as the leading scientist in the creation and development of the CCP4 program suite (Collaborative Computational Project No. 4 of the UK Research Councils) for Macromolecular Crystallography, which is now widely used by the community throughout the world and has had a huge global impact in crystallographic science. CCP4 is constantly updated and improved and is freely and easily available to the community. She also regularly tends to queries placed on the CCP4 bulletin board by students and postdocs needing help and she has also been a frequent and exellent teacher at a large number of crystallographic schools. Thus, she had a tremendous impact on all young scientists that had the priviledge of learning from her teaching, her experience and from her always open heart and friendly attitude. She has also taken on the responsibilities of being a coeditor of J Appl Cryst.
Eleanor Dodson has all the time stayed close to the biological problems. She has been involved in numerous new protein structures. A major highlight, where she had the pivotal role, was the 11-fold NCS symmetry found in the "TRAP" protein. TRAP is an RNA-binding attenuation protein. The 11-fold NCS crystallography result clarified a spread of published estimates for the number of subunits from molecular biology and biochemistry. The self rotation function and its interpretation is a masterly piece of work where Dodsonfs strengths in molecular replacement are profoundly on show.
Eleanor Dodson is an outstanding scientist who sustained very strong contributions for many years and has contributed new methods, software and structures for many years. Eleanor Dodson is highly qualified to receive the 2006 ECA Max Perutz Prize.
2004 Max Perutz Prize of the European Crystallographic Association 
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The European Crystallographic Association has awarded the 2004 Max Perutz Prize to Professor George Sheldrick
.Professor George Sheldrick is one of the most widely known crystallographers in the field. He made seminal contributions to the development of direct methods and helped to transfer the methodology into a straightforward procedure for solving small molecule structures. He has made significant contributions to structural chemistry and has published well over 700 publications in leading international, peer-reviewed journals. In recent years, his work has also become very important in biological crystallography, in the areas of structure solution based on anomalous phasing and in the refinement of protein structures at atomic resolution.
His program SHELX, which is constantly evolving, has underpinned the automation of chemical X-ray crystallography in the past three decades, and allowed the method to become a routine tool for physical and organic chemists. SHELX is the most comprehensive, reliable, and useful program for the determination and refinement of crystal structures from diffraction data. SHELX is the most cited software in crystallography and its continual use is in fact part of the foundation on which the remarkable success of our discipline rests: a large proportion of the several hundred thousands of crystal structures that have been determined owe their 'existence' to SHELX. The wealth of information available in the Cambridge Structural Database rests firmly on structures determined using his software. The free availability of the SHELX programs to the academic community has been especially important, setting a standard for others to follow. In the past fifteen years, Professor Sheldrick has focused his research on the problems of macromolecular structure determination. He has pioneered the use of direct methods for large molecules containing many atoms when atomic resolution data is available, building on the ideas of dual space refinement to provide an easy-to-use powerful phasing package in the program SHELXD. This has proved that size alone is not an insurmountable barrier when modern computing resources are exploited. This has fostered a new attitude in macromolecular crystallography by showing that with proper treatment even the biggest macromolecular structures can be refined to a level that is not very far from what has been traditionally reserved for small molecules. However, the most frequent application of SHELXD is in locating the anomalous scatterers in protein structures, a prerequisite to structure solution using anomalous phasing. His accompanying program SHELXE takes the process one step further, rapidly calculating the phases required to produce an electron density map and using a novel density modification procedure to resolve the phase ambiguity for SIR or SAD data.
George Sheldrick is head of Department for Chemistry at the University of G?ttingen. He is an excellent and dedicated teacher. His graduate students and young colleagues carry on his research traditions, and they can be found in many European laboratories. He also contributes to many workshops and training courses throughout Europe. His lucid lectures, and his deep understanding of crystallography delight students, and other participants.
George Sheldrick's contributions to crystallography have previously been recognized by many international awards including:
The previous laureates are
2000 Prof. Ada Yonath , Weizmann Institute of Science in Israel
2001 Prof. Jochen R. Schneider, HASYLAB at DESY in Germany
2003 Prof. Carmelo Giacovazzo, University of Bari, Italy
ECA Prize 2003 to Professor
Carmelo Giacovazzo TOP
The European Crystallographic Association is to award the third European Crystallography Prize to Prof. Carmelo Giacovazzo of the University of Bari, Italy. Prof. Giacovazzo is being recognized for his major theoretical and practical contributions to the solution of the phase problem in a wide spectrum of applications.
The European Crystallography Prize, which includes a monetary award as well as a certificate of recognition, will be presented during the Opening Ceremony of the upcoming 21st European Crystallographic Meeting to be held in Durban, South Africa, August 24-29, at which Prof. Giacovazzo will describe the work for which he is being honoured.
Members of the European Crystallography Prize Committee, who were appointed by the Executive Committee of the European Crystallographic Association are: Professor Davide Viterbo (Coordinator), University of Piemonte Orientale, Italy; Professor Leonid Aslanov, University of Moscow, Russia; Professor Boris Kamenar, University of Zagreb, Croatia; Professor Åke Kvick, European Synchrotron Radiation Facility, Grenoble, France; Professor Dino Moras, University of Strasbourg, France; Professor Jochen Schneider, HASYLAB at DESY, Hamburg, Germany; Professor Xavier Solans, University of Barcelona, Spain.
Prof. Giacovazzo was born in Locorotondo (Bari), Italy and studied Physics in Bari. He is Full Professor of Mineralogy at the University of Bari and Director of the CNR Institute of Crystallography. After a first period dedicated to the study of defects in minerals, he has devoted his research interests do the development of Direct Methods for the solution of the phase problem. His main theoretical contributions are the Representation Theory and several probabilistic formulae for the estimate of structure invariants and seminvariants. From the practical point of view he has directed and coordinated a research group for the implementation of widely used computer programs for the solution of crystal structures not only from single crystal data but also from powder diffraction data. More recently he has developed new and powerful methods for solving ab-initio macromolecular structures using data collected at atomic resolution. He has also provided a new probabilistic approach for the location of the heavy or anomalous scatterers in SIR-MIR-SAD-MAD techniques and for the subsequent phase estimation.
ECA Prize 2001 to Professor
Jochen R. Schneider TOP
The European Crystallographic Association is to
award the second European Crystallography Prize to Prof.
Jochen R. Schneider of the HASYLAB at DESY, Hamburg,
Germany. Prof. Schneider is being recognized for his
pioneering work on the application of gamma-ray
spectroscopy and his high energy synchrotron radiation
studies, as well as his more recent involvement in the
development of the free electron laser.
The European Crystallography Prize, which includes a
monetary award as well as a certificate of recognition,
will be presented during the Opening Ceremony of the
upcoming 20th European Crystallographic Meeting to
be held in Krakow, Poland, August 25-31, at which Prof.
Schneider will describe the work for which he is being
honored.
Members of the European Crystallography Prize Committee, who were appointed by the Executive Committee of the European Crystallographic Association are: Professor Ivar Olovsson (Coordinator), University of Uppsala, Sweden; Professor Roland Boese, University of Essen, Germany; Professor Michael Glazer, University of Oxford, UK; Professor Boris Kamenar, University of Zagreb, Croatia; Professor Åke Kvick, European Synchrotron Radiation Facility, Grenoble, France; Professor Xavier Solans, University of Barcelona, Spain; Professor Ada Yonath, Weizmann Institute of Science, Israel.
Prof. Schneider was born in Burgst?t, Saxony, Germany and studied Physics in Hamburg after an education as electrical engineer. He did his PhD under the direction of Prof. H. Maier-Leibnitz at the Institute Laue-Langevin in Grenoble, France. His work on gamma-ray diffractometry and Compton scattering was performed at the Hahn-Meitner-Institut in Berlin, the synchrotron radiation work at DESY-HASYLAB in Hamburg, where he is now heavily involved in the development of free-electron lasers driven by linear accelerators. Prof. Schneider is presently Head of HASYLAB and Director of Research for Synchrotron Radiation and Free-Electron Lasers at DESY.
ECA Prize 2000 to Professor Ada
Yonath TOP
The European Crystallographic Association has awarded the first European Crystallography Prize to Professor Ada Yonath of the Weizmann Institute of Science Rehovoth, Israel and the Max-Planck Research Unit for Ribosomal Research, DESY, Hamburg, Germany, for her pioneering achievements in structural studies on the ribosome, the universal cellular organelle on which protein biosynthesis takes place.
The European Crystallography Prize has been presented at the 19th European Crystallography Meeting in Nancy, France, August 25-31, at which Professor Yonath described the work for which she is being honored.
Professor Yonath was born in Jerusalem and received her Ph.D. under the direction of Prof. Wolfie Traub at the Weizmann Institute, where she is the incumbent of the Martin A. Kimmel Chair in Structural Biology and Head of the Kimmelman Center for Biomolecular Assemblie s. Her pioneering work over many years in pursuit of the ribosome structure which she has orchestrated on an international scale, has been concentrated in Europe, with a significant portion her activity centered at the Max-Planck Research Unit in Hamburg, which she also heads.
