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Purification, crystallization and preliminary X‐ray crystallographic studies of KstR2 (ketosteroid regulatory protein) from Mycobacterium tuberculosis
Author(s) -
Dawes Stephanie S.,
Kendall Sharon L.,
Baker Edward N.,
Lott J. Shaun
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14023589
Subject(s) - ketosteroid , tetr , repressor , mycobacterium tuberculosis , crystallization , chemistry , pathogenesis , microbiology and biotechnology , biology , biochemistry , tuberculosis , gene , medicine , gene expression , isomerase , immunology , pathology , organic chemistry
KstR2 (Rv3557c) is one of two TetR‐family transcriptional repressors of cholesterol metabolism in Mycobacterium tuberculosis . The ability to degrade cholesterol fully is important for pathogenesis, and therefore this repressor was expressed, purified and crystallized. Crystals of KstR2 diffracted to better than 1.9 Å resolution and belonged to space group C 2, with unit‐cell parameters a = 72.3, b = 90.3, c = 49.7 Å, α = γ = 90, β = 128.2°.