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Title: Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides

Abstract

Monoclinic crystals of NovP, an O-methyltransferase from S. spheroides, were obtained and native X-ray data to 1.4 Å resolution were recorded. Crystals of recombinant NovP (subunit MW = 29 967 Da; 262 amino acids), an S-adenosyl-l-methionine-dependent O-methyltransferase from Streptomyces spheroides, were grown by vapour diffusion. The protein crystallized in space group P2, with unit-cell parameters a = 51.81, b = 46.04, c = 61.22 Å, β = 104.97°. Native data to a maximum resolution of 1.4 Å were collected from a single crystal at the synchrotron. NovP is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin that targets the essential bacterial enzyme DNA gyrase.

Authors:
 [1]; ;  [2];  [1]
  1. Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH (United Kingdom)
  2. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115 (United States)
Publication Date:
OSTI Identifier:
22360290
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 3; Other Information: PMCID: PMC2330194; PMID: 17329822; PUBLISHER-ID: pu5181; OAI: oai:pubmedcentral.nih.gov:2330194; 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; DNA; MONOCRYSTALS; RESOLUTION; SPACE GROUPS; SYNCHROTRONS

Citation Formats

Stevenson, Clare E. M., Freel Meyers, Caren L., Walsh, Christopher T., and Lawson, David M., E-mail: david.lawson@bbsrc.ac.uk. Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107008287.
Stevenson, Clare E. M., Freel Meyers, Caren L., Walsh, Christopher T., & Lawson, David M., E-mail: david.lawson@bbsrc.ac.uk. Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides. United Kingdom. doi:10.1107/S1744309107008287.
Stevenson, Clare E. M., Freel Meyers, Caren L., Walsh, Christopher T., and Lawson, David M., E-mail: david.lawson@bbsrc.ac.uk. Thu . "Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides". United Kingdom. doi:10.1107/S1744309107008287.
@article{osti_22360290,
title = {Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides},
author = {Stevenson, Clare E. M. and Freel Meyers, Caren L. and Walsh, Christopher T. and Lawson, David M., E-mail: david.lawson@bbsrc.ac.uk},
abstractNote = {Monoclinic crystals of NovP, an O-methyltransferase from S. spheroides, were obtained and native X-ray data to 1.4 Å resolution were recorded. Crystals of recombinant NovP (subunit MW = 29 967 Da; 262 amino acids), an S-adenosyl-l-methionine-dependent O-methyltransferase from Streptomyces spheroides, were grown by vapour diffusion. The protein crystallized in space group P2, with unit-cell parameters a = 51.81, b = 46.04, c = 61.22 Å, β = 104.97°. Native data to a maximum resolution of 1.4 Å were collected from a single crystal at the synchrotron. NovP is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin that targets the essential bacterial enzyme DNA gyrase.},
doi = {10.1107/S1744309107008287},
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}
}