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.

引用

页码：269 / 270

页数：2

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