Structural highlights
Function
[DSVD_DESVH] May play an essential role in dissimilatory sulfite reduction.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Dissimilatory sulfite reductase D (DsrD) from Desulfovibrio vulgaris has been crystallized for a neutron diffraction study. The initial crystals obtained were too small for the neutron experiment. In order to obtain a larger crystal (>1 mm3), a combination of two techniques was developed to determine the optimum crystallization conditions: a crystallization phase diagram was obtained, followed by crystal-quality assessment via X-ray diffraction. Using conditions determined in this manner, a large single crystal (1.7 mm3) of DsrD protein was subsequently grown in D(2)O solution by the macroseeding technique. A neutron diffraction experiment was carried out using the BIX-3 diffractometer at the Japan Atomic Energy Research Institute (JAERI), collecting data to 2.4 A resolution from an optimized crystal.
Crystallization and preliminary neutron analysis of the dissimilatory sulfite reductase D (DsrD) protein from the sulfate-reducing bacterium Desulfovibrio vulgaris.,Chatake T, Mizuno N, Voordouw G, Higuchi Y, Arai S, Tanaka I, Niimura N Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2306-9. Epub 2003, Nov 27. PMID:14646103[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chatake T, Mizuno N, Voordouw G, Higuchi Y, Arai S, Tanaka I, Niimura N. Crystallization and preliminary neutron analysis of the dissimilatory sulfite reductase D (DsrD) protein from the sulfate-reducing bacterium Desulfovibrio vulgaris. Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2306-9. Epub 2003, Nov 27. PMID:14646103
