PROTEIN AND VIRUS CRYSTAL-GROWTH ON INTERNATIONAL MICROGRAVITY LABORATORY-2

被引：67

作者：

KOSZELAK, S ^{[1
]}

DAY, J ^{[1
]}

LEJA, C ^{[1
]}

CUDNEY, R ^{[1
]}

MCPHERSON, A ^{[1
]}

机构：

[1] UNIV CALIF RIVERSIDE, DEPT BIOCHEM, RIVERSIDE, CA 92521 USA

来源：

BIOPHYSICAL JOURNAL | 1995年 / 69卷 / 01期

基金：

美国国家航空航天局;

关键词：

D O I：

10.1016/S0006-3495(95)79890-3

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

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.

引用

页码：13 / 19

页数：7

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