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

5-(Hydroxyethyl)-4-methylthiazole kinase from S. aureus, which is essential to vitamin B₁ metabolism, has been crystallized in space group P1. The crystals diffracted to 2.1 Å resolution. ThiM [5-(hydroxyethyl)-4-methylthiazole kinase; EC 2.7.1.50] from Staphylococcus aureus is an essential enzyme of thiamine or vitamin B₁ 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 ų Da⁻¹. Diffraction data were collected to 2.1 Å resolution using synchrotron radiation. The phase problem was solved by molecular replacement