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1zir

From Proteopedia

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(New page: 200px<br /><applet load="1zir" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zir, resolution 1.36&Aring;" /> '''Deuterated gammaE cr...)
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[[Image:1zir.gif|left|200px]]<br /><applet load="1zir" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zir.gif|left|200px]]<br /><applet load="1zir" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zir, resolution 1.36&Aring;" />
caption="1zir, resolution 1.36&Aring;" />
'''Deuterated gammaE crystallin in H2O solvent'''<br />
'''Deuterated gammaE crystallin in H2O solvent'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZIR OCA].
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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]]
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[[Category: Artero, J.B.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:29:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:01 2008''

Revision as of 14:16, 21 February 2008


1zir, resolution 1.36Å

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Deuterated gammaE crystallin in H2O solvent

Overview

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

1ZIR is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Thu Feb 21 16:16:01 2008

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