Open AccessCrystallization and preliminary X‐ray analysis of AbsC, a novel regulator of antibiotic production in Streptomyces coelicolor
Author(s) -
Stevenson Clare E. M.,
Kock Holger,
Mootien Saraspadee,
Davies Sîan C.,
Bibb Mervyn J.,
Lawson David M.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107007944
Subject(s) - streptomyces coelicolor , crystallization , regulator , monomer , recombinant dna , chemistry , streptomyces , crystallography , biology , bacteria , biochemistry , genetics , gene , polymer , organic chemistry
Crystals of recombinant AbsC (subunit MW = 18 313 Da; 158 amino acids), a novel regulator of antibiotic production from Streptomyces coelicolor , were grown by vapour diffusion. The protein crystallizes in space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 43.53, b = 121.30, c = 143.75 Å. Native data to a resolution of 2.25 Å were recorded at station PX 14.1 (Daresbury) from a single crystal. Preliminary analysis of these data suggests that the asymmetric unit contains four copies of the AbsC monomer, giving an estimated solvent content of 47.0%. AbsC belongs to the MarR family of proteins that mediate ligand‐responsive transcriptional control.