Preliminary X-ray crystallographic analysis of SMU.573, a putative sugar kinase from Streptococcus mutans.
SMU.573 from Streptococcus mutans is a structurally and functionally uncharacterized protein that was selected for structural biology studies. Native and SeMet-labelled proteins were expressed with an N-His tag in Escherichia coli BL21 (DE3) and purified by Ni2+-chelating and size-exclusion chromatography. Crystals of the SeMet-labelled protein were obtained by the hanging-drop vapour-diffusion method and a 2.5 A resolution diffraction data set was collected using an in-house chromium radiation source. The crystals belong to space group I4, with unit-cell parameters a = b = 96.53, c = 56.26 A, alpha = beta = gamma = 90 degrees.
Zhou
Yan-Feng
YF
National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, People's Republic of China.
Li
Lan-Fen
LF
Yang
Cheng
C
Liang
Yu-He
YH
Su
Xiao-Dong
XD
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D016415:Sequence Alignment; D013295:Streptococcus mutans / Q000201:enzymology*
D001426:Bacterial Proteins; D010446:Peptide Fragments; D017853:Phosphotransferases (Alcohol Group Acceptor)