Preliminary crystallographic study of Rv0372c103-234, a hypothetical protein from Mycobacterium tuberculosis

Rv0372c is a hypothetical protein in the carbon monoxide dehydrogenase (CO-DH) gene cluster of Mycobacterium tuberculosis H37Rv, which plays a crucial role in its pathogenicity. In this study, we overexpressed and purified the core domain of Rv0372c using Ni-NTA affinity chromatography followed by size-exclusion chromatography. The Rv0372c103-234 protein crystallized in the presence of 0.1 M Tris-HCl pH 8.5, 34% PEG 2000, and 0.2 M Sodium acetate. X-ray diffraction data were acquired at 1.7 A resolution and belonged to the space group P1, with unit cell parameters a = 39.25 A, b = 58.28 A, c = 79.11 A, α = 83.68°, β = 77.30°, γ = 76.89°. The calculated Mathewes coefficient was 2.30 A3/Da with a solvent content of 46.80%, indicating that four molecules were present in the asymmetric unit. The initial structural fold of the core domain of Rv0372c resembles the Rossmann fold.