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

Abstract

A novel regulator of antibiotic production in S. coelicolor, AbsC, has been crystallized in space group P2{sub 1}2{sub 1}2{sub 1}. X-ray data to 2.25 Å resolution were collected on station PX 14.1 at Daresbury. 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{sub 1}2{sub 1}2{sub 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.

Authors:
 [1]; ;  [2];  [1];  [2];  [1]
  1. Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH (United Kingdom)
  2. Department of Molecular Microbiology, John Innes Centre, Norwich NR4 7UH (United Kingdom)
Publication Date:
OSTI Identifier:
22360275
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 3; Other Information: PMCID: PMC2330176; PMID: 17329821; PUBLISHER-ID: bw5192; OAI: oai:pubmedcentral.nih.gov:2330176; Copyright (c) International Union of Crystallography 2007; This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; DIFFUSION; LIGANDS; MONOCRYSTALS; MONOMERS; PROTEINS; RESOLUTION; SOLVENTS; SPACE GROUPS

Citation Formats

Stevenson, Clare E. M., Kock, Holger, Mootien, Saraspadee, Davies, Sîan C., Bibb, Mervyn J., and Lawson, David M., E-mail: david.lawson@bbsrc.ac.uk. Crystallization and preliminary X-ray analysis of AbsC, a novel regulator of antibiotic production in Streptomyces coelicolor. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107007944.
Stevenson, Clare E. M., Kock, Holger, Mootien, Saraspadee, Davies, Sîan C., Bibb, Mervyn J., & Lawson, David M., E-mail: david.lawson@bbsrc.ac.uk. Crystallization and preliminary X-ray analysis of AbsC, a novel regulator of antibiotic production in Streptomyces coelicolor. United Kingdom. doi:10.1107/S1744309107007944.
Stevenson, Clare E. M., Kock, Holger, Mootien, Saraspadee, Davies, Sîan C., Bibb, Mervyn J., and Lawson, David M., E-mail: david.lawson@bbsrc.ac.uk. Thu . "Crystallization and preliminary X-ray analysis of AbsC, a novel regulator of antibiotic production in Streptomyces coelicolor". United Kingdom. doi:10.1107/S1744309107007944.
@article{osti_22360275,
title = {Crystallization and preliminary X-ray analysis of AbsC, a novel regulator of antibiotic production in Streptomyces coelicolor},
author = {Stevenson, Clare E. M. and Kock, Holger and Mootien, Saraspadee and Davies, Sîan C. and Bibb, Mervyn J. and Lawson, David M., E-mail: david.lawson@bbsrc.ac.uk},
abstractNote = {A novel regulator of antibiotic production in S. coelicolor, AbsC, has been crystallized in space group P2{sub 1}2{sub 1}2{sub 1}. X-ray data to 2.25 Å resolution were collected on station PX 14.1 at Daresbury. 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{sub 1}2{sub 1}2{sub 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.},
doi = {10.1107/S1744309107007944},
journal = {Acta Crystallographica. Section F},
number = Pt 3,
volume = 63,
place = {United Kingdom},
year = {Thu Mar 01 00:00:00 EST 2007},
month = {Thu Mar 01 00:00:00 EST 2007}
}
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