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

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 angstrom resolution. Preliminary diffraction analysis suggests that the crystals belonged to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 67.8, c = 174.5 angstrom, alpha = beta = 90, gamma = 120 degrees. The Matthews coefficient was calculated to be 2.44 angstrom(3) Da(-1), assuming that the crystallographic asymmetric unit contains two protein molecules.