Crystallization and Preliminary X-ray Analysis of NADH:rubredoxin Oxidoreductase from Clostridium acetobutylicum

Crystallization and Preliminary X-ray Analysis of NADH:rubredoxin Oxidoreductase from Clostridium acetobutylicum
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丙酮丁醇梭菌 NADH:红氧还蛋白氧化还原酶的结晶和初步 X 射线分析

DOI:
10.1107/s1744309109047162
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发表时间:
2010
期刊:
Acta Crystallogr
影响因子:
--
通讯作者:
Y. Niimura and Y. Higuchi
Y. Niimura and Y. Higuchi
中科院分区:
--
文献类型:
--
作者:
K. Nishikawa;Y. Shomura;S. Kawasaki;Y. Niimura and Y. Higuchi

文献摘要

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NADH:Rubredoxin oxidoreductase(NROR)是丙酮丁醇梭菌(Clostridium acetobutylicum)中的一种O2诱导蛋白,是O2和活性氧(ROS)清除剂的多功能电子供体。重组NROR在大肠杆菌中过表达并纯化至均一;随后在293 K下使用坐滴气相扩散法结晶。 初步的晶体学分析表明,晶体属于空间群P4122或P4322,晶胞参数a = B = 98.6,c = 88.3,衍射分辨率为2.1。  假设晶体中每个不对称单元含有一个分子,则计算出马修斯系数为2.7 × 3 Da-1,溶剂含量为54.1%。  
NADH:rubredoxin oxidoreductase (NROR), an O2-inducible protein, is a versatile electron donor for scavengers of O2 and reactive oxygen species (ROS) in Clostridium acetobutylicum. Recombinant NROR was overexpressed in Escherichia coli and purified to homogeneity; it was subsequently crystallized using the sitting-drop vapour-diffusion method at 293 K. Preliminary crystallographic analysis revealed that the crystals belonged to space group P4122 or P4322, with unit-cell parameters a = b = 98.6, c = 88.3 Å, and diffracted to 2.1 Å resolution. Assuming that the crystals contained one molecule per asymmetric unit, the Matthews coefficient was calculated to be 2.7 Å3 Da−1 and the solvent content to be 54.1%.