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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary crystallographic analysis of the pyruvate-ferredoxin oxidoreductase from Desulfovibrio africanus.
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Crystallization and preliminary crystallographic analysis of the pyruvate-ferredoxin oxidoreductase from Desulfovibrio africanus.

机译：结晶和初步的晶体分析pyruvate-ferredoxin氧化还原酶从非洲脱磷孤菌属。

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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 (P212121 ) crystal forms have been grown with unit-cell dimensions a = 86.1, b = 146.7, c = 212.5 A and a = 84.8, b = 144.9, c = 203.0 A. Both crystals diffract to 2.3 A resolution using synchrotron radiation.
机译：第一次,晶体的pyruvate-ferredoxin氧化还原酶(PFOR)适合x射线分析。这种酶催化,在厌氧生物,丙酮酸的关键energy-yielding反应脱羧acetylCoA。和二价金属阳离子被用来结晶的PFOR硫酸盐还原非洲细菌脱磷孤菌属。斜方晶系的(P212121)晶体形式了单胞尺寸= 86.1,=146.7, c = 212.5 = 84.8, b = 144.9, c =203.0。使用同步辐射分辨率。

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