Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 63, Part 3 (March 2007)

crystallization communications

Acta Cryst. (2007). F63, 233-235 [ doi:10.1107/S1744309107007944 ]

Crystallization and preliminary X-ray analysis of AbsC, a novel regulator of antibiotic production in Streptomyces coelicolor

C. E. M. Stevenson, H. Kock, S. Mootien, S. C. Davies, M. J. Bibb and D. M. Lawson

Abstract: 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 P2₁2₁2₁, 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.

Keywords: AbsC; Streptomyces; antibiotic production; MarR homologue; transcriptional regulation.