title: Crystallization and preliminary X-ray diffraction studies of glycerol 3-phosphate cytidylyltransferase from Staphylococcus aureus.
abstract: Glycerol 3-phosphate cytidylyltransferase from Staphylococcus aureus (TarD(Sa)) has been expressed in Escherichia coli, purified to homogeneity and crystallized. The strategy used for determining crystallization conditions employed hanging-drop sparse-matrix screens and required a combination of three different optimization approaches. Specifically, the presence or absence of cofactors needed to be surveyed, the effects of small-molecule additives required exploration and the rate of vapour-diffusion had to be varied in order to obtain crystals of TarD(Sa) suitable for diffraction studies. Crystals thus obtained belong to the space group P3(1)21, with unit-cell parameters a = b = 92.2, c = 156.1 A, and contain four TarD(Sa) molecules per asymmetric unit. The resolution limit observed for these crystals using synchrotron radiation is 3.0 A.
authors.affiliation: Antimicrobial Research Centre and Department of Biochemistry, McMaster University, 1200 Main Street West, Hamilton, Ontario L8N 3Z5, Canada.
authors.forename: V C
authors.initials: VC
authors.lastname: Yim
authors.forename: M
authors.initials: M
authors.lastname: Zolli
authors.forename: D S
authors.initials: DS
authors.lastname: Badurina
authors.forename: L
authors.initials: L
authors.lastname: Rossi
authors.forename: E D
authors.initials: ED
authors.lastname: Brown
authors.forename: A M
authors.initials: AM
authors.lastname: Berghuis
mesh_terms: D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D009713:Nucleotidyltransferases / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D013211:Staphylococcus aureus / Q000201:enzymology*
chemical_list: D011994:Recombinant Proteins; D009713:Nucleotidyltransferases; C020675:glycerol-3-phosphate cytidylyltransferase