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Title: Crystallization and preliminary X-ray analysis of a bacterial l-amino-acid oxidase from Rhodococcus opacus

Abstract

The crystallization and preliminary X-ray analysis of a bacterial l-amino acid oxidase from R. opacus is described. The homodimeric protein contains one molecule of non-covalently bound FAD per monomer. Crystals with good diffraction properties were grown in two different orthorhombic space groups (P2{sub 1}2{sub 1}2{sub 1} and C222{sub 1}). l-Amino-acid oxidases (EC 1.4.3.2) catalyse the stereospecific oxidative deamination of an l-amino-acid substrate to an α-keto acid with the production of ammonia and hydrogen peroxide. In this study, the crystallization and preliminary X-ray analysis of a bacterial l-amino-acid oxidase from Rhodococcus opacus (RoLAAO) is described. RoLAAO is a dimeric protein consisting of two identical subunits of 489 amino acids with a calculated molecular weight of 54.2 kDa and a non-covalently bound FAD molecule. RoLAAO was crystallized by the vapour-diffusion method in two different space groups: P2{sub 1}2{sub 1}2{sub 1} (unit-cell parameters a = 65.7, b = 109.7, c = 134.4 Å) and C222{sub 1} (unit-cell parameters a = 68.3, b = 88.4, c = 186.6 Å). Both crystal forms diffracted X-rays to a resolution of at least 1.6 Å.

Authors:
 [1];  [2];  [1];  [3];  [1]
  1. Institute of Biochemistry, University of Cologne, Zuelpicher Strasse 47, 50674 Cologne (Germany)
  2. Swiss Federal Institute of Environmental Science and Technology (EAWAG), Ueberlandstrasse 133, 8600 Duebendorf (Switzerland)
  3. Institute of Molecular Enzyme Technology, Heinrich-Heine University of Duesseldorf at Research Centre Juelich, 52426 Juelich (Germany)
Publication Date:
OSTI Identifier:
22356295
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 3; Other Information: PMCID: PMC2197183; PMID: 16511322; PUBLISHER-ID: fw5072; OAI: oai:pubmedcentral.nih.gov:2197183; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; AMMONIA; CRYSTALLIZATION; CRYSTALS; DIFFRACTION; DIFFUSION; HYDROGEN PEROXIDE; MOLECULAR WEIGHT; MOLECULES; MONOMERS; RESOLUTION; SPACE GROUPS; SUBSTRATES

Citation Formats

Faust, Annette, Geueke, Birgit, Niefind, Karsten, Hummel, Werner, and Schomburg, Dietmar, E-mail: d.schomburg@uni-koeln.de. Crystallization and preliminary X-ray analysis of a bacterial l-amino-acid oxidase from Rhodococcus opacus. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309106005689.
Faust, Annette, Geueke, Birgit, Niefind, Karsten, Hummel, Werner, & Schomburg, Dietmar, E-mail: d.schomburg@uni-koeln.de. Crystallization and preliminary X-ray analysis of a bacterial l-amino-acid oxidase from Rhodococcus opacus. United Kingdom. doi:10.1107/S1744309106005689.
Faust, Annette, Geueke, Birgit, Niefind, Karsten, Hummel, Werner, and Schomburg, Dietmar, E-mail: d.schomburg@uni-koeln.de. Wed . "Crystallization and preliminary X-ray analysis of a bacterial l-amino-acid oxidase from Rhodococcus opacus". United Kingdom. doi:10.1107/S1744309106005689.
@article{osti_22356295,
title = {Crystallization and preliminary X-ray analysis of a bacterial l-amino-acid oxidase from Rhodococcus opacus},
author = {Faust, Annette and Geueke, Birgit and Niefind, Karsten and Hummel, Werner and Schomburg, Dietmar, E-mail: d.schomburg@uni-koeln.de},
abstractNote = {The crystallization and preliminary X-ray analysis of a bacterial l-amino acid oxidase from R. opacus is described. The homodimeric protein contains one molecule of non-covalently bound FAD per monomer. Crystals with good diffraction properties were grown in two different orthorhombic space groups (P2{sub 1}2{sub 1}2{sub 1} and C222{sub 1}). l-Amino-acid oxidases (EC 1.4.3.2) catalyse the stereospecific oxidative deamination of an l-amino-acid substrate to an α-keto acid with the production of ammonia and hydrogen peroxide. In this study, the crystallization and preliminary X-ray analysis of a bacterial l-amino-acid oxidase from Rhodococcus opacus (RoLAAO) is described. RoLAAO is a dimeric protein consisting of two identical subunits of 489 amino acids with a calculated molecular weight of 54.2 kDa and a non-covalently bound FAD molecule. RoLAAO was crystallized by the vapour-diffusion method in two different space groups: P2{sub 1}2{sub 1}2{sub 1} (unit-cell parameters a = 65.7, b = 109.7, c = 134.4 Å) and C222{sub 1} (unit-cell parameters a = 68.3, b = 88.4, c = 186.6 Å). Both crystal forms diffracted X-rays to a resolution of at least 1.6 Å.},
doi = {10.1107/S1744309106005689},
journal = {Acta Crystallographica. Section F},
number = Pt 3,
volume = 62,
place = {United Kingdom},
year = {Wed Mar 01 00:00:00 EST 2006},
month = {Wed Mar 01 00:00:00 EST 2006}
}
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