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Crystallization and preliminary X‐ray analysis of Rv1674c from Mycobacterium tuberculosis
Author(s) -
Li Jincheng,
Wang Xudong,
Gong Weimin,
Niu Chunyan,
Zhang Min
Publication year - 2015
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/s2053230x15001028
Subject(s) - mycobacterium tuberculosis , crystallization , tuberculosis , microbiology and biotechnology , medicine , biology , chemical engineering , pathology , engineering
Adaptations to hypoxia play an important role in Mycobacterium tuberculosis pathogenesis. Rv0324, which contains an HTH DNA‐binding domain and a rhodanese domain, is one of the key transcription regulators in response to hypoxia. M. tuberculosis Rv1674c is a homologue of Rv0324. To understand the interdomain interaction and regulation of the HTH domain and the rhodanese domain, recombinant Rv1674c protein was purified and crystallized by the vapour‐diffusion method. The crystals diffracted to 2.25 Å resolution. Preliminary diffraction analysis suggests that the crystals belonged to space group P 3 1 21 or P 3 2 21, with unit‐cell parameters a = b = 67.8, c = 174.5 Å, α = β = 90, γ = 120°. The Matthews coefficient was calculated to be 2.44 Å 3 Da −1 , assuming that the crystallographic asymmetric unit contains two protein molecules.