International
Tables for Crystallography Volume F Crystallography of biological macromolecules Edited by M. G. Rossmann and E. Arnold © International Union of Crystallography 2006 |
International Tables for Crystallography (2006). Vol. F. ch. 4.1, p. 91
Section 4.1.6.2. Instrumentation
a
Unité Propre de Recherche du CNRS, Institut de Biologie Moléculaire et Cellulaire, 15 rue René Descartes, F-67084 Strasbourg CEDEX, France, and bDepartment of Molecular Biology & Biochemistry, University of California at Irvine, Irvine, CA 92717, USA |
Crystallization in microgravity requires specific instrumentation (reviewed by DeLucas et al., 1994; Giegé et al., 1995; McPherson, 1996). A number of reactors have been focused on this goal, some based on current methods used on the ground (batch, dialysis, vapour diffusion), others on more microgravity-relevant approaches, such as free interface diffusion with crystallization vessels of rather large size. The instruments based on this latter method, however, generally cannot be used on earth for control experiments, since with gravity, mixing of the macromolecule and crystallizing-agent solutions occurs by convection. An interesting variation of the classical free interface diffusion system is the hardware using step-gradient diffusion (Sygusch et al., 1996). One of its advantages over more conventional systems is that it provides the possibility of uncoupling nucleation from growth by reducing supersaturation at a constant temperature once nuclei have appeared. A versatile instrument designed by the European Space Agency (ESA) and built by Dornier GmbH is the Advanced Protein Crystallization Facility or APCF (Bosch et al., 1992). The APCF was manifested on a number of US space-shuttle missions and yielded significant comparative `earth/space' results. It allows monitoring of growth kinetics and can accommodate free interface diffusion (see Fig. 4.1.2.1d), dialysis or vapour diffusion. Straightforward ground controls can be conducted with the dialysis cells. A new generation of instruments, the Protein Diagnostic Facility or PCDF, exclusively dedicated to diagnostic measurements of protein-crystal growth, is being developed by ESA and will be installed in the International Space Station (Plester et al., 1999).
References
Bosch, R., Lautenschlager, P., Potthast, L. & Stapelmann, J. (1992). Experiment equipment for protein crystallization in µg facilities. J. Cryst. Growth, 122, 310–316.Google ScholarDeLucas, L. J., Long, M. M., Moore, K. M., Rosenblum, W. M., Bray, T. L., Smith, C., Carson, M., Narayana, S. V. L., Harrington, M. D., Carter, D., Clark, A. D. Jr, Nanni, R. G., Ding, J., Jacobo-Molina, A., Kamer, G., Hughes, S. H., Arnold, E., Einspahr, H. M., Clancy, L. L., Rao, G. S. J., Cook, P. F., Harris, B. G., Munson, S. H., Finzel, B. C., McPherson, A., Weber, P. C., Lewandowski, F. A., Nagabhushan, T. L., Trotta, P. P., Reichert, P., Navia, M. A., Wilson, K. P., Thomson, J. A., Richards, R. N., Bowersox, K. D., Meade, C. J., Baker, E. S., Bishop, S. P., Dunbar, B. J., Trinh, E., Prahl, J., Sacco, A. Jr & Bugg, C. E. (1994). Recent results and new developments for protein crystal growth in microgravity. J. Cryst. Growth, 135, 183–195.Google Scholar
Giegé, R., Drenth, J., Ducruix, A., McPherson, A. & Saenger, W. (1995). Crystallogenesis of biological macromolecules. Biological, microgravity, and other physico-chemical aspects. Prog. Cryst. Growth Charact. 30, 237–281.Google Scholar
McPherson, A. (1996). Macromolecular crystal growth in microgravity. Crystallogr. Rev. 6, 157–305.Google Scholar
Plester, V., Stapelmann, J., Potthast, L. & Bosch, R. (1999). The protein crystallization facility, a new European instrument to investigate biological macromolecular crystal growth on board the International Space Station. J. Cryst. Growth, 196, 638–648.Google Scholar
Sygusch, J., Coulombe, R., Cassanto, J. M., Sportiello, M. G. & Todd, P. (1996). Protein crystallization in low gravity by step gradient diffusion method. J. Cryst. Growth, 162, 167–172.Google Scholar