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- W2020941487 abstract "Protein disulfide-bond formation is poorly understood in the pathogenic bacterium Mycobacterium tuberculosis. Rv2874 is the M. tuberculosis homologue of the disulfide-bond electron transporter DsbD from Escherichia coli. Both proteins share a core central transmembrane domain and a C-terminal thioredoxin domain. To investigate the possible role of Rv2874 in disulfide-bond formation in M. tuberculosis, the C-terminal domain of Rv2874 has been cloned, expressed, purified and crystallized. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 109.7, b = 118.3, c = 122.9 A, and diffract to at least 3.0 A." @default.
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- W2020941487 date "2005-02-01" @default.
- W2020941487 modified "2023-10-03" @default.
- W2020941487 title "Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from<i>Mycobacterium tuberculosis</i>" @default.
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- W2020941487 doi "https://doi.org/10.1107/s1744309105001909" @default.
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