Purification, crystallization and preliminary X-ray diffraction analysis of ThiM from Staphylococcus aureus

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt 4):479-81. doi: 10.1107/S1744309111004192. Epub 2011 Mar 25.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Phosphotransferases (Alcohol Group Acceptor) / chemistry*
  • Phosphotransferases (Alcohol Group Acceptor) / isolation & purification
  • Staphylococcus aureus / enzymology*

Substances

  • 4-methyl-5-(beta-hydroxyethyl)thiazole kinase
  • Phosphotransferases (Alcohol Group Acceptor)