Subunit composition, crystallization and preliminary crystallographic studies of the Desulfovibrio gigas aldehyde oxidoreductase containing molybdenum and [2Fe‐2S] centers

Maria J. Romão, Belarmino A. S. Barata, Margarida Archer, Karin Lobeck, Isabel Moura, Maria A. CARRONDO, Jean LeGall, Friedrich Lottspeich, Robert Huber, José J. G. Moura

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Abstract

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.

Original languageEnglish
Pages (from-to)729-732
Number of pages4
JournalEuropean Journal Of Biochemistry
Volume215
Issue number3
DOIs
Publication statusPublished - 1 Jan 1993

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