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Protein and virus crystal growth on international microgravity laboratory-2.

机译:在国际微重力实验室2上蛋白质和病毒晶体的生长。

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摘要

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.
机译:在1994年7月的国际微重力实验室2(IML-2)任务期间,在微重力中结晶了2种T = 1和1种T = 3植物病毒以及一种蛋白质。在欧洲,这种方法采用的是液-液扩散法。航天局的高级蛋白质结晶设施(APCF)。观察到萝卜黄花叶病毒(TYMV)晶体和六角型canavalin晶体在习惯上的显着变化。在微重力作用下生产的立方卫星烟草花叶病毒(STMV)的晶体大于实验室中晶体体积的30倍。 X射线衍射分析表明,如相对威尔逊图所判断,canavalin晶体形式和立方STMV晶体都衍射到更高的分辨率,并且具有优异的衍射特性。据推测,在微重力下生长的晶体周围建立准稳定的耗尽区是导致自我调控和更有序生长的原因。

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