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Updated: Apr 16, 2026

Separation and Fractionation of Cell Wall and Cell Membrane Proteins from Mycobacterium tuberculosis for Downstream Protein Analysis
Published on: September 26, 2025
Crystallization and preliminary X-ray analysis of Rv1674c from Mycobacterium tuberculosis
Jincheng Li1, Xudong Wang2, Weimin Gong2
1School of Life Sciences, Anhui University, Hefei, Anhui 230601, People's Republic of China.
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.

