Abstract
The crystallisation by counterdiffusion is a very efficient technique for obtaining high-quality protein crystals. A prerequisite for the use of counterdiffusion techniques is that mass transport must be controlled by diffusion alone. Sedimentation and convection can be avoided by either working in gelled systems, working in systems of small dimensions, or in the absence of gravity. We present the results from experiments performed on the ISS using the Protein Microscope for the International Space Station (PromISS), using digital holography to visualise crystal growth processes. We extensively characterised three model proteins for these experiments (cablys3*lysozyme, triose phosphate isomerase, and parvalbumin) and used these to assess the ISS as an environment for crystallisation by counterdiffusion. The possibility to visualise growth and movement of crystals in different types of experiments (capillary counterdiffusion and batch-type) is important, as movement of crystals is clearly not negligible.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Reference List
Zagalsky, P. F., Wright, C. E., andParsons, M.: Crystallization of laphacrustacyanin, the lobster carapace astaxanthin-protein: results from EURECA., Adv.Space Res. vol. 16, pp. 91–94 (1995).
Vergara, A., Lorber, B., Zagari, A., andGiege, R.: Physical aspects of protein crystal growth investigated with the Advanced Protein Crystallization Facility in reduced-gravity environments, Acta Crystallographica Section D-Biological Crystallography vol. 59, pp. 2–15 (2003).
Snell, E. H. andHelliwell, J. R.: Macromolecular crystallization in microgravity, Rep.Prog.Phys. vol. 68, pp. 799–853 (2005).
Chayen, N. andHelliwell, J. R.: Protein crystallizationj in microgravity: are we reaping the full benefit of outer space?, Annal.New York Academy of Sciences vol. 594, pp. 591–597 (2002).
Ng, J. D., Gavira, J. A., andGarcia-Ruiz, J. M.: Protein crystallization by capillary counterdiffusion for applied crystallographic structure determination, Journal of Structural Biology vol. 142, pp. 218–231 (2003).
Maes, D., Gonzalez-Ramirez, L. A., Lopez-Jaramillo, J., Yu, B., De Bondt, H., Zegers, I., Afonina, E., Garcia-Ruiz, J. M., andGulnik, S.: Structural study of the type II 3-dehydroquinate dehydratase from Actinobacillus pleuropneumoniae, Acta Crystallogr.D.Biol.Crystallogr. vol. 60, pp. 463–471 (2004).
Otalora, F. andGarciaRuiz, J. M.: Computer model of the diffusion reaction interplay in the gel acupuncture method, Journal of Crystal Growth vol. 169, pp. 361–367 (1996).
Carotenuto, L., Piccolo, C., Castagnolo, D., Lappa, M., Tortora, A., andGarcia-Ruiz, J. M.: Experimental observations and numerical modelling of diffusion-driven crystallisation processes, Acta Crystallographica Section D-Biological Crystallography vol. 58, pp. 1628–1632 (2002).
Dubois, F., Joannes, L., andLegros, J. C.: Improved three-dimensional imaging with a digital holography microscope with a source of partial spatial coherence, Applied Optics vol. 38, pp. 7085–7094 (12-1-1999).
Dubois, F., Requena, M. L. N., Minetti, C., Monnom, O., andIstasse, E.: Partial spatial coherence effects in digital holographic microscopy with a laser source, Applied Optics vol. 43, pp. 1131–1139 (2-10-2004).
Garcia-Ruiz, J. M., Drenth, J., Ries-Kautt, M., and Tardieu, A: Physical sciences and applications — Macromolecular crystallisation, pp. 159–171 (2001).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Zegers, I., Carotenuto, L., Evrard, C. et al. Counterdiffusion protein crystallisation in microgravity and its observation with PromISS (protein microscope for the international space station). Microgravity Sci. Technol 18, 165–169 (2006). https://doi.org/10.1007/BF02870402
Issue Date:
DOI: https://doi.org/10.1007/BF02870402