title: Protein preparation, crystallization and preliminary X-ray crystallographic studies of Smu.1392c from Streptococcus mutans.
abstract: 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.
authors.affiliation: Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Beijing, 100049, China.
authors.forename: Zeng-Qiang
authors.initials: ZQ
authors.lastname: Gao
authors.forename: Hai-Feng
authors.initials: HF
authors.lastname: Hou
authors.forename: Yu-He
authors.initials: YH
authors.lastname: Liang
authors.forename: Lan-Fen
authors.initials: LF
authors.lastname: Li
authors.forename: Xiao-Dong
authors.initials: XD
authors.lastname: Su
authors.forename: Yu-Hui
authors.initials: YH
authors.lastname: Dong
mesh_terms: 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*
chemical_list: D000123:Acetyltransferases