Protein preparation, crystallization and preliminary X-ray crystallographic analysis of N-acetylglutamate kinase from Streptococcus mutans

被引：0
|
作者：
Wu, Chang-Wei [1 ,2 ]
Li, Lan-Fen [2 ]
Liu, Xiang [2 ]
Gao, Xiong-Zhuo [1 ]
Lei, Jian [2 ]
Su, Xiao-Dong [2 ]
Zhao, Xiaojun [1 ]
Liang, Yu-He [2 ]
机构：
[1] Sichuan Univ, W China Hosp, Inst Nanobiomed Technol & Membrane Biol, Chengdu 610065, Sichuan, Peoples R China
[2] Peking Univ, Coll Life Sci, Natl Lab Prot Engn & Plant Genet Engn, Beijing 100871, Peoples R China
来源：
PROTEIN AND PEPTIDE LETTERS | 2008年 / 15卷 / 05期
基金：
中国国家自然科学基金;
关键词：
Streptococcus mutans; N-acetylglutamate kinase (NAGK); arginine biosynthesis; protein crystallography;
D O I：
10.2174/092986608784567519
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The N-acetylglutamate kinase from Streptococcus mutans was expressed in Escherichia coli in soluble form and purified to homogeneity. Crystals suitable for X-ray diffraction were obtained by hanging-drop vapor diffusion method and diffracted to 2.06 angstrom. The crystal belonged to space group P2(1)2(1)2, with unit cell parameters a = 57.19 angstrom, b =94.76 angstrom, c =47.58 angstrom. The gel filtration and initial phasing results showed that the enzyme exists as a monomer, which is different from previously reported N-acetylglutamate kinases.
引用
收藏
页码：541 / 543
页数：3
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