title: Crystallization and preliminary neutron analysis of the dissimilatory sulfite reductase D (DsrD) protein from the sulfate-reducing bacterium Desulfovibrio vulgaris.
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.
authors.affiliation: Neutron Structural Biology, Neutron Science Research Center, Japan Atomic Energy Research Institute, Tokai, Ibaraki 319-1195, Japan.
authors.forename: Toshiyuki
authors.initials: T
authors.lastname: Chatake
authors.forename: Nobuhiro
authors.initials: N
authors.lastname: Mizuno
authors.forename: Gerrit
authors.initials: G
authors.lastname: Voordouw
authors.forename: Yoshiki
authors.initials: Y
authors.lastname: Higuchi
authors.forename: Shigeki
authors.initials: S
authors.lastname: Arai
authors.forename: Ichiro
authors.initials: I
authors.lastname: Tanaka
authors.forename: Nobuo
authors.initials: N
authors.lastname: Niimura
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D016969:Desulfovibrio vulgaris / Q000201:enzymology*; D050885:Hydrogensulfite Reductase; D033363:Neutron Diffraction; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000737:chemistry*
chemical_list: D050862:Oxidoreductases Acting on Sulfur Group Donors; D050885:Hydrogensulfite Reductase