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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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Experimental techniques: data collection and analysis

Experimental techniques: data collection and analysis

(p.362) 11 Experimental techniques: data collection and analysis
Crystals, X-rays and Proteins

Dennis Sherwood

Jon Cooper

Oxford University Press

This chapter covers the essential methods by which X-rays are generated in the laboratory and at synchrotron sources for data collection from protein crystals. The methods by which X-rays of a suitable wavelength are selected and collimated for a diffraction experiment are described along with the underlying physical principles. The commonly used methods for protein data collection are then described with a summary of various area detector systems that are widely used in the field. The principles and practice of determining the X-ray diffraction intensities are then covered along with the physical basis of various correction factors which are applied to the data. The processes of scaling and merging, which allow a set of unique diffraction intensities to be obtained from the numerous redundant measurements made in a data collection, are described, along with methods for assessing the quality of the data. The effects which thermal motion and disorder within the crystal have on the diffraction intensities are discussed and appropriate correction factors are described along with a number of caveats, such as crystal twinning, which affect the subsequent steps of structure analysis.

Keywords:   X-ray sources, diffraction experiment, scaling, merging, rotation method, area detectors, data processing, auto-indexing, mosaic spread, intensity

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