| Autor: |
Romäo, 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. |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 8/1/93, Vol. 215 Issue 3, p729-732, 4p |
| Abstrakt: |
The Desulfovibrio gigas aldehyde to oxidoreductase contains molybdenum bound to a pterin cofactor and [2Fe-2S] centers. The enzyme was characterized by SDS/PAGE, gel-filtration and analytical untracentrifugation experiments. Its was crystallized at 4 °C, pH 7.2, using isopropanol and MgCl2 as precipitants. The crystals diffract beyond 0.3-nm (3.0-Å) resolution and belong to space group P6122 or its enantiomorph, with cell dimensions a = b = 14.45 nm and c = 16.32 nm. There is one sub unit/asymmetric unit which gives a packing density of 2.5 × 10 3nm3/Da (2.5 Å3/Da), consistent with the experimental crystal density, p = 1.14 g/cm3. One dimmer (approximately 2 × 100 kDa) is located on a crystallographic twofold axis. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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