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Crystals, X-rays and ProteinsComprehensive Protein Crystallography$
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Dennis Sherwood and Jon Cooper

Print publication date: 2010

Print ISBN-13: 9780199559046

Published to Oxford Scholarship Online: January 2011

DOI: 10.1093/acprof:oso/9780199559046.001.0001

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Complementary diffraction methods

Complementary diffraction methods

(p.595) 16 Complementary diffraction methods
Crystals, X-rays and Proteins

Dennis Sherwood

Jon Cooper

Oxford University Press

Many of the biological functions of proteins depend on hydrogen atoms, or protons. Whilst the X-ray diffraction data obtained from most protein crystals do not allow the positions of hydrogen atoms to be determined experimentally, some crystals diffract to atomic resolution and these allow the electron density for individual hydrogen atoms to be seen. A more powerful means for defining hydrogen atom positions is to use neutrons, rather than X-rays, in a diffraction experiment, although this generally relies on the availability of large crystals. Neutrons are much more sensitive to hydrogen atoms than X-rays and the visibility of hydrogens can be further enhanced by replacing them with the isotope deuterium, either by soaking the crystals or by special expression methods (known as perdeuteration). This chapter discusses the essential physical properties of neutrons, the basis of neutron production and diffraction, and the practical aspects of data collection and analysis. It also describes X-ray methods for analysing short-lived reaction intermediates that rely on extremely rapid data collection (the Laue method).

Keywords:   atomic resolution, unrestrained refinement, neutron protein crystallography, deuterium, reactor, spallation source, time-of-flight analysis, data collection, perdeuteration, Laue diffraction

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