title: Purification, crystallization and preliminary X-ray diffraction analysis of ThiM from Staphylococcus aureus.
abstract: ThiM [5-(hydroxyethyl)-4-methylthiazole kinase; EC 2.7.1.50] from Staphylococcus aureus is an essential enzyme of thiamine or vitamin B(1) metabolism and has been crystallized by the vapour-diffusion method. The crystals belonged to the primitive space group P1, with unit-cell parameters a = 62.06, b = 62.40, c = 107.82 Å, α = 92.25, β = 91.37, γ = 101.48° and six protomers in the unit cell, corresponding to a packing parameter V(M) of 2.3 Å(3) Da(-1). Diffraction data were collected to 2.1 Å resolution using synchrotron radiation. The phase problem was solved by molecular replacement.
authors.affiliation: Department of Chemistry, c/o DESY, Laboratory for Structural Biology of Infection and Inflammation, University of Hamburg, Building 22A, Notkestrasse 85, D-22603 Hamburg, Germany.
authors.forename: Julia
authors.initials: J
authors.lastname: Drebes
authors.forename: Markus
authors.initials: M
authors.lastname: Perbandt
authors.forename: Carsten
authors.initials: C
authors.lastname: Wrenger
authors.forename: Christian
authors.initials: C
authors.lastname: Betzel
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry* / Q000302:isolation & purification; D013211:Staphylococcus aureus / Q000201:enzymology*
chemical_list: C108435:4-methyl-5-(beta-hydroxyethyl)thiazole kinase; D017853:Phosphotransferases (Alcohol Group Acceptor)