Publication
Article Metrics
Citations
Online attention
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
PMID:
17565176
Authors:
Roberto
Steiner
(King's College London)
,
Ursula
Frerichs-deeken
,
Susan
Fetzner
(Westfalian Wilhelms-University Muenster)
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
Subject Areas:
Chemistry,
Medicine
Instruments:
I03-Macromolecular Crystallography
,
I04-Macromolecular Crystallography
Other Facilities: ESRF
Discipline Tags:
Technical Tags: