Publication Date:
1989-11-03
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeLucas, L J -- Smith, C D -- Smith, H W -- Vijay-Kumar, S -- Senadhi, S E -- Ealick, S E -- Carter, D C -- Snyder, R S -- Weber, P C -- Salemme, F R -- New York, N.Y. -- Science. 1989 Nov 3;246(4930):651-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Alabama, Center for Macromolecular Crystallography, Birmingham 35294.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2510297" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Crystallization
;
Interferon-gamma
;
Isocitrate Lyase
;
Pancreatic Elastase
;
*Proteins
;
Space Flight
;
Swine
;
*Weightlessness
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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