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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, ? = 92.25, ? = 91.37, ? = 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.

SUBMITTER: Drebes J

PROVIDER: S-EPMC3080155 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature

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

Drebes Julia J Perbandt Markus M Wrenger Carsten C Betzel Christian C

Acta crystallographica. Section F, Structural biology and crystallization communications 20110325 Pt 4

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 re ...[more]

PMID: 21505246

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