Tables for
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

International Tables for Crystallography (2006). Vol. F, ch. 10.2, p. 202   | 1 | 2 |

Section 10.2.1. Introduction

D. W. Rodgersa*

aDepartment of Biochemistry, Chandler Medical Center, University of Kentucky, 800 Rose Street, Lexington, KY 40536-0298, USA
Correspondence e-mail:

10.2.1. Introduction

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The ability to collect X-ray data from macromolecular crystals at cryogenic temperatures has played a key role in the more widespread and effective use of crystallography as a tool for biological research. Radiation-damage rates are greatly reduced at low temperature, often by orders of magnitude, making it possible to work with crystals that would otherwise diffract too weakly or decay too quickly. In particular, this radiation protection is essential for the full use of increasingly powerful synchrotron-radiation sources, and the coupling of the two permits the investigation of ever larger macromolecular complexes and the collection of higher-resolution data from nearly all samples. Cryogenic data collection has also allowed efficient experimental phasing using multiple-wavelength methods, as well as preservation of unstable samples and trapping of transient enzyme intermediates, an area that will undoubtedly continue to gain in importance.

In this chapter, practical aspects of cryocrystallography are discussed, with an emphasis on techniques and devices for crystal preparation and handling. A number of prior reviews covering these and other aspects of macromolecular cryocrystallography are available (Hope, 1988[link], 1990[link]; Watenpaugh, 1991[link]; Rodgers, 1994[link], 1997[link]; Abdel-Meguid et al., 1996[link]; Garman & Schneider, 1997[link]; Parkin & Hope, 1998[link]). Radiation-damage protection at low temperature, which is not well understood, has also been discussed (Henderson, 1990[link]; Gonzalez & Nave, 1994[link]; Rodgers, 1996[link]; Garman & Schneider, 1997[link]), and the principles and operation of cryostats for sustained cooling during data collection are described elsewhere (Rudman, 1976[link]; Hope, 1990[link]; Garman & Schneider, 1997[link]).


Abdel-Meguid, S. S., Jeruzalmi, D. & Sanderson, M. R. (1996). Crystallographic methods and protocols, edited by C. Jones, B. Mulloy & M. R. Sanderson, pp. 55–87. New Jersey: Humana Press.
Garman, E. F. & Schneider, T. R. (1997). Macromolecular cryocrystallography. J. Appl. Cryst. 30, 211–237.
Gonzalez, A. & Nave, C. (1994). Radiation damage in protein crystals at low temperature. Acta Cryst. D50, 874–877.
Henderson, R. (1990). Cryoprotection of protein crystals against radiation damage in electron and X-ray diffraction. Proc. R. Soc. London Ser. B, 241, 6–8.
Hope, H. (1988). Cryocrystallography of biological macromolecules: a generally applicable method. Acta Cryst. B44, 22–26.
Hope, H. (1990). Crystallography of biological macromolecules at ultra-low temperature. Annu. Rev. Biophys. Biophys. Chem. 19, 107–126.
Parkin, S. & Hope, H. (1998). Macromolecular cryocrystallography: cooling, mounting, storage and transportation of crystals. J. Appl. Cryst. 31, 945–953.
Rodgers, D. W. (1994). Cryocrystallography. Structure, 2, 1135–1140.
Rodgers, D. W. (1996). Cryocrystallography of macromolecules. Synchrotron Radiat. News, 9, 4–11.
Rodgers, D. W. (1997). Practical cryocrystallography. Methods Enzymol. 276, 183–203.
Rudman, R. (1976). Low-temperature X-ray diffraction. New York: Plenum Press.
Watenpaugh, K. D. (1991). Macromolecular crystallography at cryogenic temperatures. Curr. Opin. Struct. Biol. 1, 1012–1015.

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