Crystallization and preliminary X-ray analysis of S-ribosylhomocysteinase from Streptococcus mutans.
S-Ribosylhomocysteinase (LuxS) encoded by the luxS gene from Streptococcus mutans plays a crucial role in the quorum-sensing system. LuxS was solubly expressed in Escherichia coli with high yield. The purity of the purified target protein, which was identified by SDS-PAGE and MALDI-TOF MS analysis, was >95%. The protein was crystallized using the hanging-drop vapour-diffusion method with PEG 3350 as the primary precipitant. X-ray diffraction data were collected at Beijing Synchrotron Radiation Facility (BSRF). Diffraction by the crystal extended to 2.4 Å resolution and the crystal belonged to space group C222(1), with unit-cell parameters a = 55.3, b = 148.7, c = 82.8 Å.
School of Stomatology, Jilin University, Changchun, Jilin, People's Republic of China.
Hui
H
Li
Hongyan
H
Zhao
Laikuan
L
Zhu
Lihua
L
Hong
Hong
H
Zhang
Fanjing
F
Lin
Chunyan
C
Xu
Shentao
S
Li
Zhimin
Z
Zhang
D001426:Bacterial Proteins / Q000737:chemistry*; D013437:Carbon-Sulfur Lyases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D013295:Streptococcus mutans / Q000201:enzymology*
D001426:Bacterial Proteins; D013437:Carbon-Sulfur Lyases; C117753:LuxS protein, Bacteria