International
Tables for Crystallography Volume F Crystallography of biological molecules Edited by M. G. Rossmann and E. Arnold © International Union of Crystallography 2006 |
International Tables for Crystallography (2006). Vol. F. ch. 8.1, p. 165
Section 8.1.8.1. Atomic and ultra high resolution macromolecular crystallography
aDepartment of Chemistry, University of Manchester, M13 9PL, England |
The use of high SR intensity, cryo-freezing of a protein crystal to largely overcome radiation damage and sensitive, automatic area detectors (CCDs and/or image plates) is allowing diffraction data to be recorded at resolutions equivalent to smaller molecule (chemical) crystallography. In a growing number of protein crystal structure studies, atomic resolution (1.2 Å or better) is achievable (Dauter et al., 1997). The `X-ray data to parameter' ratio can be favourable enough for single and double bonds, e.g. in carboxyl side chains, to be resolved [Fig. 8.1.8.1; Deacon et al. (1997) for concanavalin A at 0.94 Å resolution]. Along with this bond distance precision, one can see the reactive proton directly. This approach complements H/D exchange neutron diffraction studies. Neutron studies have recently expanded in scope by employing Laue geometry in a synergistic development with SR Laue diffraction (Helliwell & Wilkinson, 1994; Helliwell, 1997b; Habash et al., 1997, 2000). The scope and accuracy of protein crystal structures has been transformed.
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