Abstract
Knowledge of protein crystal perfection in theory and practice is reviewed. X-ray methods of assessing perfection such as mosaicity, topography and reciprocal-space mapping are described. X-ray diffraction physics applications of protein crystals such as in Laue geometry, the large-angle oscillation technique and forming polychromatic profiles across diffraction spots are covered. Cryo- and room-temperature cases are discussed including in X-ray and neutron protein crystallography. Experience of freezing very large crystals, which are commonly used today in neutron protein crystallography, is highlighted. © 2005 International Union of Crystallography - all rights reserved.
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CITATION STYLE
Helliwell, J. R. (2005). Protein crystal perfection and its application. In Acta Crystallographica Section D: Biological Crystallography (Vol. 61, pp. 793–798). https://doi.org/10.1107/S0907444905001368
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