Cloning, expression, purification, crystallization and X-ray crystallographic analysis of ScpB (Rv1710) from Mycobacterium tuberculosis.
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 A at a synchrotron beamline. The crystal belongs to the hexagonal space group R32, with unit-cell parameters a = b = 136.69, c = 78.55 A, gamma = 120 degrees . With one molecule per asymmetric unit, the crystal volume per unit protein weight (V(M)) is 2.95 A(3) Da(-1). The structure was solved by the single anomalous dispersion method and structure refinement is in progress.
Kwon
Soo Young
SY
Beamline Division, Pohang Accelerator Laboratory, Pohang, Kyungbuk 790-784, Republic of Korea.
Kang
Beom Sik
BS
Kim
Myung Hee
MH
Kim
Kyung Jin
KJ
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D009169:Mycobacterium tuberculosis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins