1WQ2
Neutron Crystal Structure Of Dissimilatory Sulfite Reductase D (DsrD)
Summary for 1WQ2
| Entry DOI | 10.2210/pdb1wq2/pdb |
| Related | 1UCR |
| Descriptor | Protein dsvD, SULFATE ION (3 entities in total) |
| Functional Keywords | neutron hydrogen hydration protein, unknown function |
| Biological source | Desulfovibrio vulgaris |
| Total number of polymer chains | 2 |
| Total formula weight | 17779.90 |
| Authors | Chatake, T.,Mizuno, N.,Voordouw, G.,Higuchi, Y.,Arai, S.,Tanaka, I.,Niimura, N. (deposition date: 2004-09-19, release date: 2005-09-19, Last modification date: 2023-10-25) |
| Primary citation | 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.,Sect.D, 59:2306-2309, 2003 Cited by PubMed Abstract: 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. PubMed: 14646103DOI: 10.1107/S0907444903020596 PDB entries with the same primary citation |
| Experimental method | NEUTRON DIFFRACTION (2.4 Å) |
Structure validation
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