1zgt: Difference between revisions

Line 1:

[[Image:1zgt.gif|left|200px]]<br /><applet load="1zgt" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1zgt.gif|left|200px]]<br /><applet load="1zgt" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1zgt, resolution 1.45Å" />

'''Structure of hydrogenated rat gamma E crystallin in H2O'''<br />

==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.

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==

1ZGT 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=1ZGT OCA].

1ZGT 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=1ZGT OCA].

==Reference==

Line 13:

[[Category: Rattus norvegicus]]

[[Category: Single protein]]

[[Category: Artero, J.B.]]

[[Category: Artero, J B.]]

[[Category: Hartlein, M.]]

[[Category: McSweeney, S.]]

Line 20:

[[Category: 4 greek key motifs]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 07:26:~~36 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:15:23 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1zgt.gif|left|200px]]<br /><applet load="1zgt" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1zgt.gif|left|200px]]<br /><applet load="1zgt" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1zgt, resolution 1.45&Aring;" />
 '''Structure of hydrogenated rat gamma E crystallin in H2O'''<br />
 ==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.
+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==
-ZGT 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=1ZGT OCA].
+ZGT 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=1ZGT OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Rattus norvegicus]]
 [[Category: Single protein]]
-[[Category: Artero, J.B.]]
+[[Category: Artero, J B.]]
 [[Category: Hartlein, M.]]
 [[Category: McSweeney, S.]]
@@ Line 20: / Line 20: @@
 [[Category: 4 greek key motifs]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:26:36 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:15:23 2008''