Crystallization and preliminary X-ray crystallographic analysis of carboxyl-terminal region 4 of SigR from Streptomyces coelicolor A3(2).

ABSTRACT: Full-length SigR from Streptomyces coelicolor A3(2) was overexpressed in Escherichia coli, purified and submitted to crystallization trials using either polyethylene glycol 3350 or 4000 as a precipitant. X-ray diffraction data were collected to 2.60?Å resolution under cryoconditions using synchrotron X-rays. The crystal packs in space group P4?2?2, with unit-cell parameters a=b=42.14, c=102.02?Å. According to the Matthews coefficient, the crystal asymmetric unit cannot contain the full-length protein. Molecular replacement with the known structures of region 2 and region 4 as independent search models indicates that the crystal contains only the -35 element-binding carboxyl-terminal region 4 of full-length SigR. Mass-spectrometric analysis of the harvested crystal confirms this, suggesting a crystal volume per protein weight (VM) of 2.24?Å3?Da(-1) and 45.1% solvent content.

SUBMITTER: Kim KY 

PROVIDER: S-EPMC4051528 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature