产气克雷伯菌CysB蛋白（属于LysR家族）的一个DNA和N - 乙酰丝氨酸结合片段（第1至233位氨基酸残基）的结晶。

Crystallization of a DNA and N-acetylserine binding fragment (residues 1 to 233) of Klebsiella aerogenes CysB protein, a member of the LysR family.

作者信息

Tyrrell R, Davies G J, Wilson K S, Wilkinson A J

机构信息

Department of Chemistry, University of York.

出版信息

J Mol Biol. 1994 Jan 21;235(3):1159-61. doi: 10.1006/jmbi.1994.1069.

DOI:10.1006/jmbi.1994.1069

PMID:8289319

Abstract

CysB protein is a positive regulator of transcription of genes involved in cysteine biosynthesis in bacteria and a member of the LysR family of DNA binding proteins. A 233-residue N-terminal chymotryptic fragment of the protein, with DNA and N-acetylserine binding activity, has been crystallized in the presence of monomethyl-polyethylene glycol 750. The crystals diffract to 2.5 A (1 A = 0.1 nm) spacing on a rotating copper anode X-ray source and to 2.1 A spacing using synchrotron radiation and are suitable for structural studies. The space group is P2(1)2(1)2 with unit cell dimensions of a = 68.8 A, b = 109.9 A and c = 33.5 A. On the assumption that the asymmetric unit comprises one monomer, the crystals have a solvent content of approximately 50%.

摘要

CysB蛋白是细菌中参与半胱氨酸生物合成的基因转录的正调控因子，也是DNA结合蛋白的LysR家族成员。该蛋白一个含233个残基的N端胰凝乳蛋白酶片段具有DNA和N - 乙酰丝氨酸结合活性，已在单甲基聚乙二醇750存在下结晶。这些晶体在旋转铜阳极X射线源上衍射至2.5埃（1埃 = 0.1纳米）间距，使用同步辐射时衍射至2.1埃间距，适合进行结构研究。空间群为P2(1)2(1)2，晶胞尺寸为a = 68.8埃，b = 109.9埃，c = 33.5埃。假设不对称单元包含一个单体，则晶体的溶剂含量约为50%。