丙酮丁醇梭菌中NADH：铁氧化还原蛋白氧化还原酶的结晶及初步X射线分析
Crystallization and preliminary X-ray analysis of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum.
作者信息
Nishikawa Koji, Shomura Yasuhito, Kawasaki Shinji, Niimura Youichi, Higuchi Yoshiki
机构信息
Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):23-5. doi: 10.1107/S1744309109047162. Epub 2009 Dec 25.
Abstract
NADH
rubredoxin oxidoreductase (NROR), an O(2)-inducible protein, is a versatile electron donor for scavengers of O(2) 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 P4(1)22 or P4(3)22, with unit-cell parameters a = b = 98.6, c = 88.3 A, and diffracted to 2.1 A resolution. Assuming that the crystals contained one molecule per asymmetric unit, the Matthews coefficient was calculated to be 2.7 A(3) Da(-1) and the solvent content to be 54.1%.
摘要
NADH
铁氧化还原蛋白氧化还原酶（NROR）是一种受O₂诱导的蛋白质，是丙酮丁醇梭菌中O₂和活性氧（ROS）清除剂的通用电子供体。重组NROR在大肠杆菌中过表达并纯化至同质；随后在293K下使用坐滴气相扩散法进行结晶。初步晶体学分析表明，晶体属于空间群P4(1)22或P4(3)22，晶胞参数a = b = 98.6，c = 88.3 Å，衍射分辨率为2.1 Å。假设每个不对称单元包含一个分子，计算出的马修斯系数为2.7 ų Da⁻¹，溶剂含量为54.1%。
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