Crystallization and preliminary X-ray analysis of Escherichia coli peptidyl-tRNA hydrolase

被引：0
|
作者：
Schmitt, E
Fromant, M
Plateau, P
Mechulam, Y
Blanquet, S
机构：
[1] Laboratoire de Biochimie, Unite de Rech. Associee 1970, Ecole Polytechnique
来源：
PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1997年 / 28卷 / 01期
关键词：
crystallization; X-ray structure; peptidyl-tRNA hydrolase;
D O I：
10.1002/(SICI)1097-0134(199705)28:1<135::AID-PROT14>3.0.CO;2-K
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Peptidyl-tRNA hydrolase from Escherichia coli, a monomer of 21 kDa, was overexpressed from its cloned gene pth and crystallized by using polyethylene glycol as precipitant. The crystals are orthorhombic and have unit cell parameters a = 47.24 Angstrom b = 63.59 Angstrom and c = 62.57 Angstrom. They belong. to space group P2(1)2(1)2(1) and diffract to better than 1.2 Angstrom resolution. The structure is being solved by multiple isomorphous replacement. (C) 1997 Wiley-Liss, Inc.
引用
收藏
页码：135 / 136
页数：2
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