Preparation, crystallization and preliminary X-ray analysis of threonine synthase from Streptococcus mutans.
The thrC gene of Streptococcus mutans encodes threonine synthase, which is a potential target for drug design. To study the structure and function of the enzyme, the thrC gene was amplified from Streptococcus mutans genomic DNA and cloned into the expression vector pET28alpha. The protein 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. The crystal diffracted to 2.5 A and belonged to space group P3(1) or P3(2), with unit cell parameters a=b=60.39 A, c=118.62 A.
Tang
De-Wei
DW
Institute for Nanobiomedical Technology and Membrane Biology, West China Hospital, Sichuan University, Chengdu, Sichuan, China.
Li
Lan-Fen
LF
Yu
Ya-Mei
YM
Liu
Xiang-Yu
XY
Su
Xiao-Dong
XD
Zhao
Xiaojun
X
Liang
Yu-He
YH
D000595:Amino Acid Sequence; D019757:Carbon-Oxygen Lyases / Q000737:chemistry* / Q000302:isolation & purification*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D013295:Streptococcus mutans / Q000201:enzymology*
D019757:Carbon-Oxygen Lyases; C023160:threonine synthase