Protein and virus crystal growth on international microgravity laboratory-2.
Two T = 1 and one T = 3 plant viruses, along with a protein, were crystallized in microgravity during the International Microgravity Laboratory-2 (IML-2) mission in July of 1994. The method used was liquid-liquid diffusion in the European Space Agency's Advanced Protein Crystallization Facility (APCF). Distinctive alterations in the habits of Turnip Yellow Mosaic Virus (TYMV) crystals and hexagonal canavalin crystals were observed. Crystals of cubic Satellite Tobacco Mosaic Virus (STMV) more than 30 times the volume of crystals grown in the laboratory were produced in microgravity. X-ray diffraction analysis demonstrated that both crystal forms of canavalin and the cubic STMV crystals diffracted to significantly higher resolution and had superior diffraction properties as judged by relative Wilson plots. It is postulated that the establishment of quasi-stable depletion zones around crystals growing in microgravity are responsible for self-regulated and more ordered growth.
Koszelak
S
S
Department of Biochemistry, University of California, Riverside 92521, USA.
Day
J
J
Leja
C
C
Cudney
R
R
McPherson
A
A
D003460:Crystallization; D003574:Cytochrome c Group / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry; D014027:Tobacco Mosaic Virus / Q000254:growth & development*; D017806:Tymovirus / Q000254:growth & development*; D014764:Viral Proteins / Q000737:chemistry* / Q000302:isolation & purification; D014893:Weightlessness
D003574:Cytochrome c Group; D010940:Plant Proteins; D014764:Viral Proteins; C006882:canavalin protein, Canavalia ensiformis