Crystallization and preliminary X‐ray crystallographic analysis of carboxyl‐terminal region 4 of SigR from Streptomyces coelicolor A3(2). Issue 6 (1st June 2014)

• Record Type: Journal Article
• Authors: Kim, Keon Young; Kim, Sunmin; Park, Jeong Kuk; Song, HyoJin; Park, SangYoun
• Is Part Of: Acta crystallographica. Volume 70:Issue 6(2014:Jun.)
• Page Start: 747
• Page End: 749
• Publication Date: 2014-06-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14008437
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Full‐length SigR from <italic>Streptomyces coelicolor</italic> A3(2) was overexpressed in <italic>Escherichia coli</italic>, 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 <italic>P</italic>4₃2₁2, with unit‐cell parameters <italic>a</italic> = <italic>b</italic> = 42.14, <italic>c</italic> = 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 (<italic>V</italic>_M) of 2.24 ų Da⁻¹ and 45.1% solvent content.</p> </abstract>