Open AccessSubunit composition, crystallization and preliminary crystallographic studies of the Desulfovibrio gigas aldehyde oxidoreductase containing molybdenum and [2Fe‐2S] centers
Author(s) -
ROMÃO Maria J.,
BARATA Belarmino A. S.,
ARCHER Margarida,
LOBECK Karin,
MOURA Isabel,
CARRONDO Maria A.,
LeGALL Jean,
LOTTSPEICH Friedrich,
HUBER Robert,
MOURA José J. G.
Publication year - 1993
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1993.tb18085.x
Subject(s) - dimer , crystallography , oxidoreductase , pterin , molybdenum , chemistry , crystallization , aldehyde , cofactor , desulfovibrio , crystal (programming language) , protein subunit , stereochemistry , enzyme , inorganic chemistry , organic chemistry , catalysis , biochemistry , programming language , gene , computer science , sulfate
The Desulfovibrio gigas aldehyde oxidoreductase contains molybdenum bound to a pterin cofactor and [2Fe‐2S] centers. The enzyme was characterized by SDS/PAGE, gel‐filtration and analytical ultracentrifugation experiments. It was crystallized at 4°C, pH 7.2, using isopropanol and MgCl 2 as precipitants. The crystals diffract beyond 0.3‐nm (3.0‐Å) resolution and belong to space group P6 1 22 or its enantiomorph, with cell dimensions a = b = 14.45 nm and c = 16.32 nm. There is one subunit/asymmetric unit which gives a packing density of 2.5 × 10 −3 nm 3 /Da (2.5 Å 3 /Da), consistent with the experimental crystal density, p = 1.14 g/cm 3 . One dimer (approximately 2 × 100 kDa) is located on a crystallographic twofold axis.