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Science 3 November 1989:
Vol. 246. no. 4930, pp. 651 - 654
DOI: 10.1126/science.2510297
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Articles

Science, Vol 246, Issue 4930, 651-654
Copyright © 1989 by American Association for the Advancement of Science

articles

Protein crystal growth in microgravity

LJ DeLucas, CD Smith, HW Smith, S Vijay-Kumar, SE Senadhi, SE Ealick, DC Carter, RS Snyder, PC Weber, FR Salemme, and al. et

University of Alabama, Center for Macromolecular Crystallography, Birmingham 35294.

The crystals of most proteins or other biological macromolecules are poorly ordered and diffract to lower resolutions than those observed for most crystals of simple organic and inorganic compounds. Crystallization in the microgravity environment of space may improve crystal quality by eliminating convection effects near growing crystal surfaces. A series of 11 different protein crystal growth experiments was performed on U.S. space shuttle flight STS-26 in September 1988. The microgravity-grown crystals of gamma-interferon D1, porcine elastase, and isocitrate lyase are larger, display more uniform morphologies, and yield diffraction data to significantly higher resolutions than the best crystals of these proteins grown on Earth.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Three-dimensional structure of recombinant human interferon-gamma.
S. Ealick, W. Cook, S Vijay-Kumar, M Carson, T. Nagabhushan, P. Trotta, and C. Bugg (1991)
Science 252, 698-702
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