来自棕色固氮菌的蛋白质X的衍射质量晶体。

Diffraction quality crystals of protein X from Azotobacter vinelandii.

作者信息

Diller T C, Shaw A, Isas J M, Burgess B K, Stout C D

机构信息

Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.

出版信息

J Mol Biol. 1994 Aug 26;241(4):620-1. doi: 10.1006/jmbi.1994.1535.

DOI:10.1006/jmbi.1994.1535

PMID:8057382

Abstract

Protein X from Azotobacter vinelandii has recently been shown to be either a NADPH oxidase or a NADP+ reductase that interacts specifically with ferredoxin I. Single crystals have been obtained by vapor diffusion from polyethylene glycol 4000 solutions containing 100 mM citrate buffer (pH 5.5). The crystals belong to space group P2(1)2(1)2 with unit cell constants a = 68.9 A, b = 76.9 A, c = 52.8 A and one molecule (M(r) 29,000) per asymmetric unit. The crystals diffract to 2.5 A resolution.

摘要

最近发现，来自棕色固氮菌的蛋白质X要么是一种与铁氧化还原蛋白I特异性相互作用的NADPH氧化酶，要么是一种NADP+还原酶。通过气相扩散法，从含有100 mM柠檬酸盐缓冲液（pH 5.5）的聚乙二醇4000溶液中获得了单晶。这些晶体属于空间群P2(1)2(1)2，晶胞参数a = 68.9 Å，b = 76.9 Å，c = 52.8 Å，每个不对称单元中有一个分子（相对分子质量为29,000）。这些晶体的衍射分辨率为2.5 Å。