Open AccessCloning, expression, purification, crystallization and X‐ray crystallographic analysis of ScpB (Rv1710) from Mycobacterium tuberculosis
Author(s) -
Kwon SooYoung,
Kang Beom Sik,
Kim Myung Hee,
Kim Kyung Jin
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107056953
Subject(s) - crystallography , monoclinic crystal system , crystallization , mycobacterium tuberculosis , crystal structure , cloning (programming) , chemistry , condensation , materials science , tuberculosis , physics , organic chemistry , pathology , computer science , programming language , thermodynamics , medicine
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 Å at a synchrotron beamline. The crystal belongs to the hexagonal space group R 32, with unit‐cell parameters a = b = 136.69, c = 78.55 Å, γ = 120°. With one molecule per asymmetric unit, the crystal volume per unit protein weight ( V M ) is 2.95 Å 3 Da −1 . The structure was solved by the single anomalous dispersion method and structure refinement is in progress.