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Title: Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rü61a: a cofactor-devoid dioxygenase of the α/β-hydrolase-fold superfamily

Abstract

Preliminary crystallographic data are reported for 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) from A. nitroguajacolicus Rü61a. 1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) is a cofactor-devoid dioxygenase that is involved in the anthranilate pathway of quinaldine degradation. HOD has been proposed to belong to the α/β-hydrolase-fold superfamily of enzymes. N-terminally His{sub 6}-tagged HOD has been crystallized by the hanging-drop vapour-diffusion method using sodium/potassium tartrate as a precipitant and CuCl{sub 2} as an additive. The structure was solved by the single anomalous dispersion (SAD) technique using data collected to 3.5 Å resolution at the Cu absorption peak wavelength. The crystals belong to the primitive tetragonal space group P4{sub 3}2{sub 1}2, with unit-cell parameters a = b = 153.788, c = 120.872 Å.

Authors:
 [1]; ;  [2];  [3]
  1. Randall Division of Cell and Molecular Biophysics, King’s College London, New Hunt’s House, Guy’s Campus, London SE1 1UL (United Kingdom)
  2. Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, D-48149 Münster (Germany)
  3. (United Kingdom)
Publication Date:
OSTI Identifier:
22360329
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 5; Other Information: PMCID: PMC2335005; PMID: 17565176; PUBLISHER-ID: gj5017; OAI: oai:pubmedcentral.nih.gov:2335005; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ABSORPTION; CRYSTALLIZATION; CRYSTALS; DIFFUSION; DISPERSIONS; OXYGEN; PEAKS; POTASSIUM; RESOLUTION; SODIUM; SPACE GROUPS; WAVELENGTHS

Citation Formats

Steiner, Roberto A., E-mail: roberto.steiner@kcl.ac.uk, Frerichs-Deeken, Ursula, Fetzner, Susanne, and Randall Division of Cell and Molecular Biophysics, King’s College London, New Hunt’s House, Guy’s Campus, London SE1 1UL. Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rü61a: a cofactor-devoid dioxygenase of the α/β-hydrolase-fold superfamily. United Kingdom: N. p., 2007. Web. doi:10.1107/S174430910701353X.
Steiner, Roberto A., E-mail: roberto.steiner@kcl.ac.uk, Frerichs-Deeken, Ursula, Fetzner, Susanne, & Randall Division of Cell and Molecular Biophysics, King’s College London, New Hunt’s House, Guy’s Campus, London SE1 1UL. Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rü61a: a cofactor-devoid dioxygenase of the α/β-hydrolase-fold superfamily. United Kingdom. doi:10.1107/S174430910701353X.
Steiner, Roberto A., E-mail: roberto.steiner@kcl.ac.uk, Frerichs-Deeken, Ursula, Fetzner, Susanne, and Randall Division of Cell and Molecular Biophysics, King’s College London, New Hunt’s House, Guy’s Campus, London SE1 1UL. Tue . "Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rü61a: a cofactor-devoid dioxygenase of the α/β-hydrolase-fold superfamily". United Kingdom. doi:10.1107/S174430910701353X.
@article{osti_22360329,
title = {Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rü61a: a cofactor-devoid dioxygenase of the α/β-hydrolase-fold superfamily},
author = {Steiner, Roberto A., E-mail: roberto.steiner@kcl.ac.uk and Frerichs-Deeken, Ursula and Fetzner, Susanne and Randall Division of Cell and Molecular Biophysics, King’s College London, New Hunt’s House, Guy’s Campus, London SE1 1UL},
abstractNote = {Preliminary crystallographic data are reported for 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) from A. nitroguajacolicus Rü61a. 1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) is a cofactor-devoid dioxygenase that is involved in the anthranilate pathway of quinaldine degradation. HOD has been proposed to belong to the α/β-hydrolase-fold superfamily of enzymes. N-terminally His{sub 6}-tagged HOD has been crystallized by the hanging-drop vapour-diffusion method using sodium/potassium tartrate as a precipitant and CuCl{sub 2} as an additive. The structure was solved by the single anomalous dispersion (SAD) technique using data collected to 3.5 Å resolution at the Cu absorption peak wavelength. The crystals belong to the primitive tetragonal space group P4{sub 3}2{sub 1}2, with unit-cell parameters a = b = 153.788, c = 120.872 Å.},
doi = {10.1107/S174430910701353X},
journal = {Acta Crystallographica. Section F},
number = Pt 5,
volume = 63,
place = {United Kingdom},
year = {Tue May 01 00:00:00 EDT 2007},
month = {Tue May 01 00:00:00 EDT 2007}
}
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