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Structural biology is key to our understanding of the mechanisms of biological processes. This book describes current methods and future frontiers in crystal growth and use of X-ray and Neutron crystallography, in the context of the very successful current automation of crystallization and generation of synchrotron X-ray and neutron beams.
The crystallization of proteins and nucleic acids and/or their complexes has become more highly automated but is still often a trial and error based approach. In parallel, a number of X-ray diffraction based techniques have been developed which explain
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Produktbeschreibung
Structural biology is key to our understanding of the mechanisms of biological processes. This book describes current methods and future frontiers in crystal growth and use of X-ray and Neutron crystallography, in the context of the very successful current automation of crystallization and generation of synchrotron X-ray and neutron beams.
The crystallization of proteins and nucleic acids and/or their complexes has become more highly automated but is still often a trial and error based approach. In parallel, a number of X-ray diffraction based techniques have been developed which explain the physical reasons limiting the resulting crystallographic data and thus show how that data may be improved. Crystal growth is also pivotal in neutron crystallography, which establishes the hydrogen and hydrationaspects. Thus this book is aimed at addressing the science behind obtaining the best and most complete structural data possible for biological macromolecules, so that the detailed structural biology and chemistry of these important molecules emerge. Crystal imperfections such as twinning and latticedisorders, as well as multiple crystal situations, and their possible remedies, are also described. The small crystal frontier in micro-crystal crystallography, crystallites in powders and finally down to the proposed single molecule structure determination of X-ray lasers are covered. Overall this interdisciplinary book will interest crystal growers, X-ray and neutron physicists and the biological crystallographers, including graduate students.
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Autorenporträt
Naomi E. Chayen is Professor of Biomedical Sciences at Imperial College London, Visiting Professor at Harvard Medical School and the President of the International Organisation for Biological Crystallization (IOBCr). She organises and chairs crystallization sessions at international conferences and courses, and is a Crystallization Co-Editor of Acta Crystallographica D. Prof J R Helliwell is Professor of Structural Chemistry at the University of Manchester and an Honorary Visiting Scientist at the STFC Daresbury Laboratory. He has served as Editor-in-Chief of Acta Crystallographica and is currently President of the European Crystallographic Association. Dr Edward Snell is Assistant Professor at the Hauptman-Woodward Medical Research Institute at the State University of New York at Buffalo. He has worked at NASA as a senior scientist and was PI on several space missions on the International Space station. He has received a number of academic awards.
Rezensionen
A streamlined and logical summary of the sequence of procedures that a crystallographer needs to follow to obtain the structure of a protein of interest. The discussion greatly benefits from the authors' practical experience as protein crystallographers who have important structures under their belts. The Journal of the American Chemical Society