Cloning, expression, purification, crystallization and X-ray crystallographic analysis of ScpB (Rv1710) from Mycobacterium tuberculosis
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- Cloning, expression, purification, crystallization and X-ray crystallographic analysis of ScpB (Rv1710) from Mycobacterium tuberculosis
- S Y Kwon; B S Kang; Myung Hee Kim; K J Kim
- Bibliographic Citation
- Acta Crystallographica Section F-Structural Biology, vol. 63, no. 12, pp. 1058-1060
- Publication Year
- Structural maintenance of chromosome (SMC) proteins play diverse roles in cellular DNA reassembly by directly interacting with DNA. They require non-SMC proteins for their proper function; these include the conserved segregation and condensation proteins (Scps) in prokaryotes. ScpB from Mycobacterium tuberculosis was crystallized using the sitting-drop vapour-diffusion method in the presence of 2 M NaCl and 10% PEG 6000 at 295 K. X-ray diffraction data were collected to a maximum resolution of 2.3 ? at a synchrotron beamline. The crystal belongs to the hexagonal space group R32, with unit-cell parameters a = b = 136.69, c = 78.55 ?, γ = 120°. With one molecule per asymmetric unit, the crystal volume per unit protein weight (V M) is 2.95 ?3 Da-1. The structure was solved by the single anomalous dispersion method and structure refinement is in progress.
- ScpBSegregation and condensation proteins
- Int Union Crystallography
- Appears in Collections:
- Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
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