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

Acta Crystallogr Sect F Struct Biol Cryst Commun

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.

Published: April 2011

AI Article Synopsis

  • ThiM, an essential enzyme for thiamine (vitamin B1) metabolism in Staphylococcus aureus, has been successfully crystallized.
  • The crystals were found to belong to the primitive space group P1, with specific unit-cell parameters such as a = 62.06 Å and b = 62.40 Å.
  • Diffraction data were collected at a resolution of 2.1 Å using synchrotron radiation, and molecular replacement was utilized to solve the phase problem.

Article 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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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3080155PMC
http://dx.doi.org/10.1107/S1744309111004192DOI Listing

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