CRYSTALLIZATION OF PROTEIN AND RIBOSOMAL PARTICLES IN MICROGRAVITY

被引：17

作者：

TRAKHANOV, SD ^{[1
]}

GREBENKO, AI ^{[1
]}

SHIROKOV, VA ^{[1
]}

GUDKOV, AV ^{[1
]}

EGOROV, AV ^{[1
]}

BARMIN, IN ^{[1
]}

VAINSTEIN, BK ^{[1
]}

SPIRIN, AS ^{[1
]}

机构：

[1] ACAD SCI USSR,INST PROTEIN RES,MOSCOW 117333,USSR

来源：

JOURNAL OF CRYSTAL GROWTH | 1991年 / 110卷 / 1-2期

关键词：

D O I：

10.1016/0022-0248(91)90901-G

中图分类号：

O7 [晶体学];

学科分类号：

0702 ; 070205 ; 0703 ; 080501 ;

摘要：

The ability of several proteins (catalase, pyrophosphatase, aspartate aminotransferase, ceruloplasmin) as well as 30 S ribosomal subparticles to form crystals in microgravity was investigated during the "Photon" satellite mission (14-28 April 1988). Two (catalase and 30 S ribosomal subparticles) produced crystals in space. The crystals of catalase grown in microgravity were larger and showed less variation in crystal size than those obtained in a control experiment on the earth. The tendency of these crystals as well as crystals of 30 S particles to form rosettes or clusters was also reduced significantly.

引用

页码：317 / 321

页数：5

共 9 条

[1] 3-DIMENSIONAL STRUCTURE AT 5-A RESOLUTION OF CYTOSOLIC ASPARATATE TRANSAMINASE FROM CHICKEN HEART [J].