Newcomers to the field of structural biology, which aims to understand life at the molecular level, see a vast number of existing results and are faced with a diverse range of experimental methods. These are used singly or in various combinations, however the uncertainties of the results found are unfortunately not fully assessed. Beginning with the basic physics of describing systematic and random errors, this book aims to explore these uncertainties, by examining the accuracy of each experimental method used to determine a 3D biological macromolecule structure and its dynamics, and their various possible combinations. The book also discusses the uncertainties in our determination of atomic positions in our static structures, and our analysis of the living cell. Aimed at graduate students from a wide range of science disciplines including physics, chemistry, biology, and mathematics, this book provides an overview of the topic of precision and accuracy in biological crystallography, diffraction, scattering, microscopies, and spectroscopies.
Les mer
Aimed at postgraduate students from a wide range of science disciplines including physics, chemistry, biology, and mathematics, this book is a teaching book on the whole topic of precision and accuracy in biological crystallography, diffraction, scattering, microscopies, and spectroscopies.
Les mer
Preface Acknowledgements About the author 1: Introduction 2: The physics of errors as illustrated by X-ray crystallography 3: History of the reliability of structure determination methods 4: Mass spectrometry 5: Structure validation approaches 6: Other validation tools: Round-robin projects 7: Similarities and differences in the probes used in structure determination 8: Fibre diffraction 9: Powder diffraction 10: Small-angle solution scattering 11: Electron microscopy (EM) 12: X-ray absorption spectroscopy (XAS) 13: NMR 14: EPR for metalloproteins 15: Combining methods for accuracy 16: Combining methods to span different length scales 17: Role of simulations of structural dynamics as a complement to experimental studies 18: Role of predictions as a grand challenge in biology: Protein fold prediction is solved 19: A new method: X-ray photon correlation spectroscopy (XPCS) to study biocondensed matter 20: Conclusions 21: Appendix A1: Bayesian reasoning in data analysis and model refinement Bibliography Abbreviations List Index
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John R. Helliwell studied physics at the University of York and obtained a PhD from the University of Oxford in 1978. For many years he was closely associated with the Synchrotron Radiation Source at Daresbury Laboratory, while also holding positions at the University of Keele, the University of York and the University of Manchester, where he is now an Emeritus Professor. His research has contributed to over 100 Protein Data Bank crystal structure depositions spanning enzymes, lectins and crustacyanins with ligands such as saccharides, carotenoids and metallodrugs or metalloimaging agents. In 2014 he was awarded the A. L. Patterson Award by the American Crystallographic Association and in 2015 he was awarded the Max Perutz Prize by the European Crystallographic Association. He is a Fellow of the American Crystallographic Association, a Fellow of the Institute of Physics, the Royal Society of Chemistry, and the Royal Society of Biology.
Les mer
The first comprehensive treatment of uncertainties in the structures determined by all relevant experimental methods Includes an improved set of database resources, governed by data deposition policies set by experts in the field Highlights the need for new and improved methods which in turn will lead to important developments in research and equipment manufacturing
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Produktdetaljer

ISBN
9780198952824
Publisert
2025
Utgiver
Oxford University Press
Vekt
382 gr
Høyde
240 mm
Bredde
160 mm
Dybde
15 mm
Aldersnivå
UP, 05
Språk
Product language
Engelsk
Format
Product format
Innbundet
Antall sider
144

Forfatter

Biografisk notat

John R. Helliwell studied physics at the University of York and obtained a PhD from the University of Oxford in 1978. For many years he was closely associated with the Synchrotron Radiation Source at Daresbury Laboratory, while also holding positions at the University of Keele, the University of York and the University of Manchester, where he is now an Emeritus Professor. His research has contributed to over 100 Protein Data Bank crystal structure depositions spanning enzymes, lectins and crustacyanins with ligands such as saccharides, carotenoids and metallodrugs or metalloimaging agents. In 2014 he was awarded the A. L. Patterson Award by the American Crystallographic Association and in 2015 he was awarded the Max Perutz Prize by the European Crystallographic Association. He is a Fellow of the American Crystallographic Association, a Fellow of the Institute of Physics, the Royal Society of Chemistry, and the Royal Society of Biology.