AbstractBased on the results of microgravity crystallization experiments using the protein canavalin aboard four separate U.S. space shuttle missions, we present visual observations and diffraction data that support the contention that protein crystals of improved quality can be obtained in a microgravity environment. With canavalin, no significant increase in resolution was noted, but an overall improvement in diffraction quality, as judged by statistical analyses of the data, was clear. We present the hypothesis that this improvement in quality may be due primarily to the elimination of defects and dislocations rather than an overall enhancement of order. We further suggest that the mechanism for this improvement may be microgravity stabilized depletion zones that develop around growing crystals that establish and maintain optimal growth conditions more rapidly following nucleation. Such zones would be destroyed by convective flow effects in earth's gravity.
The effect of microgravity on protein crystal growth
Advances in Space Research ; 11 , 7 ; 343-356
1991-01-01
14 pages
Article (Journal)
Electronic Resource
English
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