首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Cloning expression purification crystallization and preliminary X-ray diffraction analysis of a ferredoxin/flavodoxin-NADP(H) oxidoreductase (Bc0385) from Bacillus cereus
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Cloning expression purification crystallization and preliminary X-ray diffraction analysis of a ferredoxin/flavodoxin-NADP(H) oxidoreductase (Bc0385) from Bacillus cereus

机译:蜡状芽孢杆菌铁氧还蛋白/黄酮毒素-NADP(H)氧化还原酶(Bc0385)的克隆表达纯化结晶和初步X射线衍射分析

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摘要

Ferredoxin/flavodoxin-NADP(H) oxidoreductases (FNRs) are key enzymes involved in catalysing electron transfer between ferredoxins/flavodoxins and NAD(P)H/NAD(P)+. In Bacillus cereus there are three genes that may encode FNRs, and the Bc0385 FNR has been cloned, overexpressed, purified and successfully crystallized in its NADPH/NADP+-free form. Diffraction data have been collected to 2.5 Å resolution from crystals belonging to the orthorhombic space group P21212, with unit-cell parameters a = 57.2, b = 164.3, c = 95.0 Å, containing two FNR molecules in the asymmetric unit. The structure of the Bc0385 FNR has been solved by molecular replacement, and is a member of the homodimeric thioredoxin reductase-like class of FNRs.
机译:铁氧还蛋白/黄酮毒素-NADP(H)氧化还原酶(FNRs)是催化铁氧还蛋白/黄酮毒素与NAD(P)H / NAD(P) + 之间电子转移的关键酶。在蜡状芽孢杆菌中,有三个基因可以编码FNR,而Bc0385 FNR已被克隆,过表达,纯化并以其NADPH / NADP + 游离形式成功结晶。已从正交晶体空间群P21212的晶体中收集到衍射数据,分辨率为2.5Å,其晶胞参数a = 57.2,b = 164.3,c = 95.0Å,在不对称单元中包含两个FNR分子。 Bc0385 FNR的结构已通过分子置换解决,并且是FNRs的同二聚体硫氧还蛋白还原酶样类的成员。

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