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Crystallization and preliminary X-ray analysis of Rv1674c from Mycobacterium tuberculosis.

ABSTRACT: 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 P3121 or P3221, with unit-cell parameters a = b = 67.8, c = 174.5?Å, ? = ? = 90, ? = 120°. The Matthews coefficient was calculated to be 2.44?Å(3)?Da(-1), assuming that the crystallographic asymmetric unit contains two protein molecules.

SUBMITTER: Li J

PROVIDER: S-EPMC4356315 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of Rv1674c from Mycobacterium tuberculosis.

Li Jincheng J Wang Xudong X Gong Weimin W Niu Chunyan C Zhang Min M

Acta crystallographica. Section F, Structural biology communications 20150228 Pt 3

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. ...[more]

PMID: 25760714

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