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

International Tables for Crystallography (2006). Vol. F, ch. 10.1, pp. 197-201   | 1 | 2 |

Chapter 10.1. Introduction to cryocrystallography

H. Hopea*

aDepartment of Chemistry, University of California, Davis, One Shields Ave, Davis, CA 95616-5295, USA
Correspondence e-mail:


Bald, W. B. (1984). The relative efficiency of cryogenic fluids used in the rapid quench cooling of biological samples. J. Microsc. 134, 261–270.
Bellamy, H. D., Phizackerley, R. P., Soltis, S. M. & Hope, H. (1994). An open-flow cryogenic cooler for single-crystal diffraction experiments. J. Appl. Cryst. 27, 967–970.
Douzou, P., Hui Bon Hoa, G. & Petsko, G. A. (1975). Protein crystallography at sub-zero temperatures: lysozyme–substrate complexes in cooled mixed solutions. J. Mol. Biol. 96, 367–380.
Esnouf, R. M., Ren, J., Garman, E. F., Somers, D. O'N., Ross, C. K., Jones, E. Y., Stammers, D. K. & Stuart, D. I. (1998). Continuous and discontinuous changes in the unit cell of HIV-1 reverse transcriptase crystals on dehydration. Acta Cryst. D54, 938–953.
Fu, Z.-Q., Du Bois, G. C., Song, S. P., Harrison, R. W. & Weber, I. T. (1999). Improving the diffraction quality of MTCP-1 crystals by post-crystallization soaking. Acta Cryst. D55, 5–7.
Garman, E. F. & Mitchell, E. P. (1996). Glycerol concentrations required for cryoprotection of 50 typical protein crystallization solutions. J. Appl. Cryst. 29, 584–587.
Götz, G., Mészáros, E. & Vali, G. (1991). Atmospheric particles and nuclei, p. 142. Budapest: Akadémiai Kiadó.
Hope, H.(1988). Cryocrystallography of biological macromolecules: a generally applicable method. Acta Cryst. B44, 22–26.
Hope, H. (1990). Cryocrystallography of biological macromolecules at ultra-low temperature. Annu. Rev. Biophys. Biophys. Chem. 19, 107–126.
Hope, H., Frolow, F., von Böhlen, K., Makowski, I., Kratky, C., Halfon, Y., Danz, H., Webster, P., Bartels, K. S., Wittmann, H. G. & Yonath, A. (1989). Cryocrystallography of ribosomal particles. Acta Cryst. B45, 190–199.
Hui Bon Hoa, G. & Douzou, P. (1973). Ionic strength and protein activity of supercooled solutions used in experiments with enzyme systems. J. Biol. Chem. 248, 4649–4654.
Mitchell, E. P. & Garman, E. F. (1994). Flash freezing of protein crystals: investigation of mosaic spread and diffraction limit with variation of cryoprotectant concentration. J. Appl. Cryst. 27, 1070–1074.
Parkin, S. & Hope, H. (1998). Macromolecular cryocrystallography: cooling, mounting, storage and transportation of crystals. J. Appl. Cryst. 31, 945–953.
Petsko, G. A. (1975). Protein crystallography at sub-zero temperatures: cryoprotective mother liquors for protein crystals. J. Mol. Biol. 96, 381–392.
Post, B., Schwartz, R. S. & Fankuchen, I. (1951). An improved device for X-ray diffraction studies at low temperatures. Rev. Sci. Instrum. 22, 218–220.
Ryan, K. P. (1992). Cryofixation of tissues for electron microscopy: a review of plunge cooling methods. Scanning Microsc. 6, 715–743.
Schreuder, H. A., Groendijk, H., van der Lan, J. M. & Wierenga, R. K. (1988). The transfer of protein crystals from their original mother liquor to a solution with a completely different precipitant. J. Appl. Cryst. 21, 426–429.
Travers, F. & Douzou, P. (1970). Dielectric constants of alcoholic-water mixtures at low temperature. J. Phys. Chem. 74, 2243–2244.
Vali, G. (1995). In Biological ice nucleation and its applications, edited by R. E. Lee Jr, G. J. Warren & L. V. Gusta, pp. 1–28. St Paul: APS Press.
Walker, L. J., Moreno, P. O. & Hope, H. (1998). Cryocrystallography: effect of cooling medium on sample cooling rate. J. Appl. Cryst. 31, 954–956.