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

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1999年 / 55卷

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

页码：329 / 331

页数：3

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