Open AccessPurification, crystallization and preliminary X‐ray diffraction analysis of ThiM from Staphylococcus aureus
Author(s) -
Drebes Julia,
Perbandt Markus,
Wrenger Carsten,
Betzel Christian
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111004192
Subject(s) - crystallization , staphylococcus aureus , x ray , x ray crystallography , crystallography , materials science , diffraction , microbiology and biotechnology , physics , chemistry , biology , optics , bacteria , thermodynamics , genetics
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 P 1, 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.