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Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a: a cofactor-devoid dioxygenase of the alpha/beta hydrolase-fold superfamily

DOI: 10.1107/S174430910701353X DOI Help
PMID: 17565176 PMID Help

Authors: Roberto A. Steiner (King's College London) , Ursula Frerichs-Deeken (Westfälische Wilhelms-Universität Münster) , Susan Fetzner (Westfälische Wilhelms-Universität Münster)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 63 , PAGES 382-385

State: Published (Approved)
Published: May 2007
Diamond Proposal Number(s): 1220

Abstract: 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 [alpha]/[beta]-hydrolase-fold superfamily of enzymes. N-terminally His6-tagged HOD has been crystallized by the hanging-drop vapour-diffusion method using sodium/potassium tartrate as a precipitant and CuCl2 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 P43212, with unit-cell parameters a = b = 153.788, c = 120.872 Å.

Journal Keywords: Oxygenase; Cofactor-Free; [Alpha]/[Beta]-Hydrolase; 1H-3-Hydroxy-4-Oxoquinaldine; Sad

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Other Facilities: ID14-EH1, BM30 at ESRF

Added On: 27/09/2010 15:35

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)