CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF THE HUMAN ERYTHROCYTE BISPHOSPHOGLYCERATE MUTASE

被引：6
|
作者：
CHERFILS, J [1 ]
ROSA, R [1 ]
GAREL, MC [1 ]
CALVIN, MC [1 ]
ROSA, J [1 ]
JANIN, J [1 ]
机构：
[1] HOP HENRI MONDOR, CNRS, UA 607, INSERM, U91, F-94010 CRETEIL, FRANCE
来源：
JOURNAL OF MOLECULAR BIOLOGY | 1991年 / 218卷 / 02期
关键词：
D O I：
10.1016/0022-2836(91)90710-N
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：
Bisphosphoglycerate mutase (EC 2.7.5.4) catalyzes the synthesis and breakdown of 2,3-diphosphoglycerate in red cells. The human enzyme, cloned and expressed in Escherichia coli has been crystallized in the rhombohedral space group R32 with a = b = c = 100·4 A ̊ and α = β = γ = 81·2 °. The asymmetric unit contains either a dimeric enzyme molecule or a monomer. © 1991.
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页码：269 / 270
页数：2
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