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 P212121, with unit‐cell parameters a = 43.53, b = 121.30, c = 143.75 Å. Native data...

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Veröffentlicht in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2007-03, Vol.63 (3), p.233-235
Hauptverfasser: Stevenson, Clare E. M., Kock, Holger, Mootien, Saraspadee, Davies, Sîan C., Bibb, Mervyn J., Lawson, David M.
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Sprache:eng
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Zusammenfassung: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.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309107007944