Protein preparation, crystallization and preliminary X-ray crystallographic analysis of N-acetylglutamate kinase from Streptococcus mutans.
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 A. The crystal belonged to space group P2(1)2(1)2, with unit cell parameters a = 57.19 A, b =94.76 A, c =47.58 A. The gel filtration and initial phasing results showed that the enzyme exists as a monomer, which is different from previously reported N-acetylglutamate kinases.
Wu
Chang-Wei
CW
Institute for Nanobiomedical Technology and Membrane Biology, West China Hospital, Sichuan University, Chengdu 610065, Sichuan, China. zhaoxj@scu.edu.cn.
Li
Lan-Fen
LF
Liu
Xiang
X
Gao
Xiong-Zhuo
XZ
Lei
Jian
J
Su
Xiao-Dong
XD
Zhao
Xiaojun
X
Liang
Yu-He
YH
D003460:Crystallization; D018360:Crystallography, X-Ray; D017851:Phosphotransferases (Carboxyl Group Acceptor) / Q000737:chemistry* / Q000302:isolation & purification*; D013295:Streptococcus mutans / Q000201:enzymology*
D017851:Phosphotransferases (Carboxyl Group Acceptor); C018721:acetylglutamate kinase