Crystallization and preliminary X-ray analysis of AbsC, a novel regulator of antibiotic production in Streptomyces coelicolor.
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 P2(1)2(1)2(1), with unit-cell parameters a = 43.53, b = 121.30, c = 143.75 A. Native data to a resolution of 2.25 A 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.
Stevenson
Clare E M
CE
Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, England.
Kock
Holger
H
Mootien
Saraspadee
S
Davies
Sîan C
SC
Bibb
Mervyn J
MJ
Lawson
David M
DM
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000096:biosynthesis*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D008969:Molecular Sequence Data; D048372:Streptomyces coelicolor / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins