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  • Title: Crystallization and preliminary X-ray analysis of Rv1674c from Mycobacterium tuberculosis.
    Author: Li J, Wang X, Gong W, Niu C, Zhang M.
    Journal: Acta Crystallogr F Struct Biol Commun; 2015 Mar; 71(Pt 3):354-7. PubMed ID: 25760714.
    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, 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.
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