1wq2: Difference between revisions

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==Overview==
==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 (>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 (>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==
==About this Structure==
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[[Category: neutron hydrogen hydration protein]]
[[Category: neutron hydrogen hydration protein]]


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Revision as of 13:47, 21 February 2008

File:1wq2.gif


1wq2, resolution 2.4Å

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Neutron Crystal Structure Of Dissimilatory Sulfite Reductase D (DsrD)

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 (>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

1WQ2 is a Single protein structure of sequence from Desulfovibrio vulgaris with SO4 and DOD as ligands. Full crystallographic information is available from OCA.

Reference

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

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