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• W2037153911 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 P4₃2₁2, 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." @default.
• W2037153911 created "2016-06-24" @default.
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• W2037153911 date "2014-05-10" @default.
• W2037153911 modified "2023-09-26" @default.
• W2037153911 title "Crystallization and preliminary X-ray crystallographic analysis of carboxyl-terminal region 4 of SigR from<i>Streptomyces coelicolor</i>A3(2)" @default.
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• W2037153911 doi "https://doi.org/10.1107/s2053230x14008437" @default.
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