Protein preparation, crystallization and preliminary X-ray crystallographic studies of Smu.1392c from Streptococcus mutans.
Smu.1392c is a protein with 158 residues of uncharacterized function. Bioinformatics studies predict it is a putative acetyltransferase. In order to identify its exact function via structural studies, Smu.1392c gene was amplified from Streptococcus mutans genomic DNA and cloned into expression vector PET28a. Smu.1392c was crystallized and diffracted to a resolution of 3 A in-house. The crystal belongs to R32 space group, with unit cell parameters a=b=229.10, c=63.49 A. There are 2 or 3 molecules in the asymmetric unit.
Gao
Zeng-Qiang
ZQ
Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Beijing, 100049, China.
Hou
Hai-Feng
HF
Liang
Yu-He
YH
Li
Lan-Fen
LF
Su
Xiao-Dong
XD
Dong
Yu-Hui
YH
D000123:Acetyltransferases / Q000737:chemistry* / Q000302:isolation & purification; D017124:Conserved Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D017434:Protein Structure, Tertiary; D013295:Streptococcus mutans / Q000201:enzymology*
D000123:Acetyltransferases