Crystallization and preliminary neutron analysis of the dissimilatory sulfite reductase D (DsrD) protein from the sulfate-reducing bacterium Desulfovibrio vulgaris.
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.
Chatake
Toshiyuki
T
Neutron Structural Biology, Neutron Science Research Center, Japan Atomic Energy Research Institute, Tokai, Ibaraki 319-1195, Japan.
Mizuno
Nobuhiro
N
Voordouw
Gerrit
G
Higuchi
Yoshiki
Y
Arai
Shigeki
S
Tanaka
Ichiro
I
Niimura
Nobuo
N
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*
D050862:Oxidoreductases Acting on Sulfur Group Donors; D050885:Hydrogensulfite Reductase