Article

Expression, purification, crystallization and preliminary X-ray analysis of Rv3117, a probable thiosulfate sulfurtransferase (CysA3) from Mycobacterium tuberculosis.

Protein Structure and Function Group, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Acta Crystallographica Section F Structural Biology and Crystallization Communications (Impact Factor: 0.55). 07/2008; 64(Pt 6):541-4. DOI: 10.1107/S1744309108014449
Source: PubMed

ABSTRACT The gene product of open reading frame Rv3117 from Mycobacterium tuberculosis (Mtb) strain H37Rv is annotated as encoding a probable rhodanese-like thiosulfate sulfurtransferase (MtbCysA3). MtbCysA3 was expressed and purified and then crystallized using the sitting-drop vapour-diffusion method. X-ray diffraction data were collected and processed to a maximum resolution of 2.5 A. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 38.86, b = 91.43, c = 83.57 A, beta = 96.6 degrees . Preliminary diffraction data shows that two molecules are present in the asymmetric unit; this corresponds to a V(M) of 2.4 A(3) Da(-1).

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