Open AccessCrystallization and preliminary X‐ray crystallographic analysis of hydroquinone dioxygenase from Sphingomonas sp. TTNP3
Author(s) -
Da Vela Stefano,
Ferraroni Marta,
Kolvenbach Boris A.,
Keller Eva,
Corvini Philippe F. X.,
Scozzafava Andrea,
Briganti Fabrizio
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112012341
Subject(s) - monoclinic crystal system , crystallography , hydroquinone , dioxygenase , heterotetramer , chemistry , crystallization , sphingomonas , resolution (logic) , x ray crystallography , stereochemistry , crystal structure , enzyme , diffraction , protein subunit , organic chemistry , biochemistry , physics , 16s ribosomal rna , artificial intelligence , computer science , optics , gene
Hydroquinone dioxygenase (HQDO), a novel Fe II ring‐fission dioxygenase from Sphingomonas sp. strain TTNP3 which oxidizes a wide range of hydroquinones to the corresponding 4‐hydroxymuconic semialdehydes, has been crystallized. The enzyme is an α 2 β 2 heterotetramer constituted of two subunits of 19 and 38 kDa. Diffraction‐quality crystals of HQDO were obtained using the sitting‐drop vapour‐diffusion method at 277 K from a solution consisting of 16% PEG 4000, 0.3 M MgCl 2 , 0.1 M Tris pH 8.5. The crystals belonged to the monoclinic space group P 2 1 , with unit‐cell parameters a = 88.4, b = 125.4, c = 90.8 Å, β = 105.3°. The asymmetric unit contained two heterotetramers, i.e. four copies of each of the two different subunits related by noncrystallographic 222 symmetry. A complete data set extending to a maximum resolution of 2.5 Å was collected at 100 K using a wavelength of 0.980 Å.