Overview

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.

Full Product Details

Author:   John R. Helliwell (Emeritus Professor, Emeritus Professor, Department of Chemistry, University of Manchester)
Publisher:   Oxford University Press
Imprint:   Oxford University Press
Volume:   25
Dimensions:   Width: 16.00cm , Height: 1.50cm , Length: 24.00cm
Weight:   0.382kg
ISBN:  

9780198952824

ISBN 10:   0198952821
Pages:   144
Publication Date:   23 October 2025
Audience:   College/higher education ,  Postgraduate, Research & Scholarly
Format:   Hardback
Publisher's Status:   Active
Availability:   To order  
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Table of Contents

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 12: X-ray absorption spectroscopy 13: NMR 14: EPR for metalloproteins 15: Combining methods for accuracy 16: Combining methods to span different length scales 17: Role of simulations as a complement to experimental structural dynamics studies 18: Role of predictions as a grand challenge: protein fold prediction is solved 19: A new method: X-ray photon correlation spectroscopy to study biocondensed matter 20: Conclusions Appendix 1 - Bayesian reasoning in data analysis and model refinement

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Author Information

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.

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