Tables for
Volume C
Mathematical, physical and chemical tables
Edited by E. Prince

International Tables for Crystallography (2006). Vol. C, ch. 3.4, p. 167

Section General

P. F. Lindleya

aESRF, Avenue des Martyrs, BP 220, F-38043 Grenoble CEDEX, France General

| top | pdf |

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[link]; Hartmann et al., 1982[link]; Frauenfelder et al., 1987[link]) and, more recently, ribonuclease-A (Tilton, Dewan & Petsko, 1992[link]; Rasmussen, Stock, Ringe & Petsko, 1992[link]). 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.


Frauenfelder, H., Hartmann, H., Karplus, M., Kuntz, I. D. Jr, Kuriyan, J., Parak, F., Petsko, G. A., Ringe, D., Tilton, R. F. Jr, Conolly, M. L. & Max, N. (1987). Thermal expansion of a protein. Biochemistry, 26, 254–261.Google Scholar
Frauenfelder, H., Petsko, G. A. & Tsernoglou, D. (1979). Temperature-dependent X-ray diffraction as a probe of protein structure dynamics. Nature (London), 280, 558.Google Scholar
Hartmann, H., Parak, F., Steigemann, W., Petsko, G. A., Ringe-Ponzi, D. & Frauenfelder, H. (1982). Conformational substrates in a protein: structure and dynamics of metmyoglobin at 80 K. Proc. Natl Acad. Sci. USA, 79, 4967–4971. Google Scholar
Rasmussen, B. F., Stock, A. M., Ringe, D. & Petsko, G. A. (1992). Crystalline ribonuclease A loses function below the dynamical transition at 220 K. Nature (London), 357, 423–424.Google Scholar
Tilton, R. F. Jr, Dewan, J. C. & Petsko, G. A. (1992). Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K. Biochemistry, 31, 2469–2481. Google Scholar

to end of page
to top of page