1wq2: Difference between revisions

Revision as of 16:47, 21 February 2008

Neutron Crystal Structure Of Dissimilatory Sulfite Reductase D (DsrD)

OverviewOverview

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.

About this StructureAbout this Structure

1WQ2 is a Single protein structure of sequence from Desulfovibrio vulgaris with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 15:47:03 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 4: / Line 4: @@
 ==Overview==
-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 (&gt;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.
+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 (&gt;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.
 ==About this Structure==
@@ Line 24: / Line 24: @@
 [[Category: neutron hydrogen hydration protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:42:16 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:47:03 2008''