Literature DB >> 21505246

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

Julia Drebes1, Markus Perbandt, Carsten Wrenger, Christian Betzel.   

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.

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Year:  2011        PMID: 21505246      PMCID: PMC3080155          DOI: 10.1107/S1744309111004192

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  15 in total

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2.  Structure of ThiM from Vitamin B1 biosynthetic pathway of Staphylococcus aureus - Insights into a novel pro-drug approach addressing MRSA infections.

Authors:  Julia Drebes; Madeleine Künz; Björn Windshügel; Alexey G Kikhney; Ingrid B Müller; Raphael J Eberle; Dominik Oberthür; Huaixing Cang; Dmitri I Svergun; Markus Perbandt; Christian Betzel; Carsten Wrenger
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