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

被引:4
|
作者
Drebes, Julia [1 ,2 ]
Perbandt, Markus [1 ,3 ]
Wrenger, Carsten [2 ]
Betzel, Christian [1 ]
机构
[1] Univ Hamburg, Dept Chem, DESY, Lab Struct Biol Infect & Inflammat, D-22603 Hamburg, Germany
[2] Bernhard Nocht Inst Trop Med, Dept Biochem, D-20359 Hamburg, Germany
[3] Univ Med Ctr Hamburg Eppendorf, Dept Med Microbiol Virol & Hyg, D-20246 Hamburg, Germany
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2011年 / 67卷
关键词
ThiM; Staphylococcus aureus; 5-(hydroxyethyl)-4-methylthiazole kinase; vitamin B-1 metabolism; THIAMIN BIOSYNTHESIS; BACILLUS-SUBTILIS; INFECTIONS;
D O I
10.1107/S1744309111004192
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 A, alpha = 92.25, beta = 91.37, gamma = 101.48 degrees and six protomers in the unit cell, corresponding to a packing parameter V (M) of 2.3 A3 Da-1. Diffraction data were collected to 2.1 A resolution using synchrotron radiation. The phase problem was solved by molecular replacement.
引用
收藏
页码:479 / 481
页数:3
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