International
Tables for Crystallography Volume C Mathematical, physical and chemical tables Edited by E. Prince © International Union of Crystallography 2006 |
International Tables for Crystallography (2006). Vol. C. ch. 3.4, p. 167
|
Cryocrystallography not only minimizes the effects of radiation damage but also often allows the collection of high-quality, high-resolution data from a single specimen. In the case of very labile systems such as ribosomal particles, it is sometimes the only means of obtaining useful diffraction data. Further, cryocrystallography permits the study of temperature effects on the structure and dynamics of biological macromolecules. In this latter regard, examples include multiple-temperature crystallographic studies on sperm whale myoglobin (Frauenfelder, Petsko & Tsernoglou, 1979; Hartmann et al., 1982
; Frauenfelder et al., 1987
) and, more recently, ribonuclease-A (Tilton, Dewan & Petsko, 1992
; Rasmussen, Stock, Ringe & Petsko, 1992
). The future will no doubt see the routine emergence of cryogenic techniques for data collection, using both conventional and synchrotron X-ray sources, from biological macromolecules, with consequent improvement in structure quality and detail.
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