1zir: Difference between revisions
New page: left|200px<br /><applet load="1zir" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zir, resolution 1.36Å" /> '''Deuterated gammaE cr... |
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[[Image:1zir.gif|left|200px]]<br /><applet load="1zir" size=" | [[Image:1zir.gif|left|200px]]<br /><applet load="1zir" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1zir, resolution 1.36Å" /> | caption="1zir, resolution 1.36Å" /> | ||
'''Deuterated gammaE crystallin in H2O solvent'''<br /> | '''Deuterated gammaE crystallin in H2O solvent'''<br /> | ||
==Overview== | ==Overview== | ||
Rat gammaE-crystallin was overexpressed, purified under different | Rat gammaE-crystallin was overexpressed, purified under different labelling conditions and crystallized and X-ray data were collected at resolutions between 1.71 and 1.36 A. The structures were determined by molecular replacement. In these structures, the cd loop of the Greek-key motif 3, which is the major structural key motif of the two phase-transition groups of gamma-crystallins, presents a double conformation. The influence of the perdeuteration on the protein structure was determined by comparison of the atomic positions and temperature factors of the different models. The perdeuterated proteins have a similar structure to their hydrogenated counterparts, but partial or full deuteration may have some effect on the atomic B-factor values. | ||
==About this Structure== | ==About this Structure== | ||
1ZIR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1ZIR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZIR OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Artero, J | [[Category: Artero, J B.]] | ||
[[Category: Hartlein, M.]] | [[Category: Hartlein, M.]] | ||
[[Category: McSweeney, S.]] | [[Category: McSweeney, S.]] | ||
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[[Category: 4 greek key motifs]] | [[Category: 4 greek key motifs]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:01 2008'' |
Revision as of 17:16, 21 February 2008
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Deuterated gammaE crystallin in H2O solvent
OverviewOverview
Rat gammaE-crystallin was overexpressed, purified under different labelling conditions and crystallized and X-ray data were collected at resolutions between 1.71 and 1.36 A. The structures were determined by molecular replacement. In these structures, the cd loop of the Greek-key motif 3, which is the major structural key motif of the two phase-transition groups of gamma-crystallins, presents a double conformation. The influence of the perdeuteration on the protein structure was determined by comparison of the atomic positions and temperature factors of the different models. The perdeuterated proteins have a similar structure to their hydrogenated counterparts, but partial or full deuteration may have some effect on the atomic B-factor values.
About this StructureAbout this Structure
1ZIR is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
A comparison of refined X-ray structures of hydrogenated and perdeuterated rat gammaE-crystallin in H2O and D2O., Artero JB, Hartlein M, McSweeney S, Timmins P, Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1541-9. Epub 2005, Oct 19. PMID:16239733
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