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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary analysis of a water-forming NADH oxidase from Lactobacillus sanfranciscensis.
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Crystallization and preliminary analysis of a water-forming NADH oxidase from Lactobacillus sanfranciscensis.

机译：结晶和初步分析从乳酸菌water-forming NADH氧化酶sanfranciscensis。

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摘要

Single crystals have been obtained of NADH oxidase (Nox), a flavoenzyme cloned from Lactobacillus sanfranciscensis. The enzyme catalyzes the oxidation of two equivalents of NAD(P)H and reduces one equivalent of oxygen to yield two equivalents of water, without releasing hydrogen peroxide after the reduction of the first equivalent of NAD(P)H. The enzyme crystallizes in space group P2(1)2(1)2(1), with unit-cell parameters a = 59.6, b = 92.6, c = 163.5 A. The crystals diffract to 1.85 A resolution using synchrotron radiation. Matthews coefficient calculations suggest the presence of two molecules per asymmetric unit (V(M) = 2.3 A(3) Da(-1), 45.5% solvent content), which has been confirmed by the molecular-replacement solution using a search molecule derived from NADH peroxidase (PDB code 1f8w).
机译：取得了单晶的NADH氧化酶从乳酸菌(Nox)黄素酶克隆sanfranciscensis。氧化两种NAD (P) H和等价物减少一个等效的氧气产生两个当量的水,没有释放出氢过氧化还原后的第一位相当于NAD (P) H。空间群P2(1) 2(1) 2(1),与单胞参数= 59.6,b = 92.6, c = 163.5。晶体衍射分辨率1.85使用同步加速器辐射。计算表明两个的存在每个不对称分子单元(V (M) = 2.3 (3)Da(1), 45.5%溶剂内容)由molecular-replacement确认解决方案使用搜索来自NADH分子过氧化物酶(PDB代码1 f8w)。

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