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.
|Number of pages||4|
|Journal||European Journal of Biochemistry|
|Publication status||Published - 1 Jan 1993|