1wq2: Difference between revisions

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==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==

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[[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''

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@@ 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''