Crystallization and preliminary crystallographic analysis of the pyruvate-ferredoxin oxidoreductase from Desulfovibrio africanus

被引:7
|
作者
Pieulle, L
Chabrière, E
Hatchikian, C
Fontecilla-Camps, JC
Charon, MH
机构
[1] CNRS, Unite Bioenerget & Ingn Proteines, F-13402 Marseille 20, France
[2] CEA, CNRS, Inst Biol Struct J P Ebel, Cristallog & Cristallogenese Prot Lab, F-38027 Grenoble, France
关键词
D O I
10.1107/S0907444998008920
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
For the first time, crystals of a pyruvate-ferredoxin oxidoreductase (PFOR) suitable for X-ray analysis have been obtained. This enzyme catalyzes, in anaerobic organisms, the crucial energy-yielding reaction of pyruvate decarboxylation to acetylCoA. Polyethylene glycol and divalent metal cations have been used to crystallize the PFOR from the sulfate-reducing bacterium Desulfovibrio africanus. Two different orthorhombic (P2(1)2(1)2(1)) crystal forms have been grown with unit-cell dimensions a = 86.1, b = 146.7, c = 212.5 Angstrom and a = 84.8, b = 144.9, c = 203.0 Angstrom, Both crystals diffract to 2.3 Angstrom resolution using synchrotron radiation.
引用
收藏
页码:329 / 331
页数:3
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