大肠杆菌主要硝基还原酶的结晶及初步晶体学分析

Crystallization and preliminary crystallographic analysis of major nitroreductase from Escherichia coli.

作者信息

Kobori T, Lee W C, Akagi T, Sasaki H, Zenno S, Saigo K, Tanokura M

机构信息

Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.

出版信息

Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1901-2. doi: 10.1107/s0907444999008422.

DOI:10.1107/s0907444999008422

PMID:10531489

Abstract

NADPH

nitrocompound oxidoreductase from Escherichia coli, NfsA, has been crystallized in the presence of FMN by the vapor-diffusion method using polyethylene glycol 6000 as a precipitant. The crystals belonged to the triclinic space group P1 with cell dimensions, a = 52.2, b = 52.7, c = 53.3 A, alpha = 75.1, beta = 60.1, gamma = 60.5 degrees. The crystals are expected to contain two NfsA molecules per asymmetric unit. The crystals diffracted X-rays to at least 2.3 A resolution and are appropriate for structural analysis at high resolution.

摘要

来自大肠杆菌的NADPH：硝基化合物氧化还原酶NfsA，已通过气相扩散法，以聚乙二醇6000作为沉淀剂，在FMN存在的情况下结晶。晶体属于三斜晶系空间群P1，晶胞参数为a = 52.2、b = 52.7、c = 53.3 Å，α = 75.1°、β = 60.1°、γ = 60.5°。预计每个不对称单元包含两个NfsA分子。这些晶体的X射线衍射分辨率至少为2.3 Å，适合进行高分辨率结构分析。