4gcr: Difference between revisions

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[[Image:4gcr.jpg|left|200px]]<br /><applet load="4gcr" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:4gcr.jpg|left|200px]]<br /><applet load="4gcr" size="350" color="white" frame="true" align="right" spinBox="true"

caption="4gcr, resolution 1.47Å" />

'''STRUCTURE OF THE BOVINE EYE LENS PROTEIN GAMMA-B (GAMMA-II)-CRYSTALLIN AT 1.47 ANGSTROMS'''<br />

==Overview==

The molecular structure of calf gammaB-crystallin (previously called, gammaII), a lens-specific protein, has been refined to a crystallographic, R factor of 18.1% for all reflection data, between 8.0 and 1.47 A, 25 959, hkl measured at 293 (1) K. 230 water molecules have been defined by, difference Fourier techniques and included in a restrained least-squares, refinement. Difference Fourier maps clearly indicated the presence of, multiple sites for the sulfur atoms of Cys 18 and Cys 22 which were, therefore given coupled second-site occupancies during the refinement. The, sulfur atom in the major position of Cys 22 is in the reduced state., Either of the Cys 18 sites can form a high-energy disulfide bridge with, the minor position of Cys 22. The position of the carboxy terminus and, many other surface side chains have been further defined including the RGD, signal peptide. The hydration of the backbone and the interdomain region, has been analysed. 27 water molecules make extensive contacts to a single, protein molecule and thus contribute to its stability.

The molecular structure of calf gammaB-crystallin (previously called gammaII), a lens-specific protein, has been refined to a crystallographic R factor of 18.1% for all reflection data, between 8.0 and 1.47 A, 25 959 hkl measured at 293 (1) K. 230 water molecules have been defined by difference Fourier techniques and included in a restrained least-squares refinement. Difference Fourier maps clearly indicated the presence of multiple sites for the sulfur atoms of Cys 18 and Cys 22 which were therefore given coupled second-site occupancies during the refinement. The sulfur atom in the major position of Cys 22 is in the reduced state. Either of the Cys 18 sites can form a high-energy disulfide bridge with the minor position of Cys 22. The position of the carboxy terminus and many other surface side chains have been further defined including the RGD signal peptide. The hydration of the backbone and the interdomain region has been analysed. 27 water molecules make extensive contacts to a single protein molecule and thus contribute to its stability.

==About this Structure==

4GCR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure ~~superseeds~~ the now removed PDB entry 1GCR. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=4GCR OCA].

4GCR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry 1GCR. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GCR OCA].

==Reference==

Line 13:

[[Category: Bos taurus]]

[[Category: Single protein]]

[[Category: Blundell, T.L.]]

[[Category: Blundell, T L.]]

[[Category: Driessen, H.P.C.]]

[[Category: Driessen, H P.C.]]

[[Category: Lindley, P.]]

[[Category: Moss, D.S.]]

[[Category: Moss, D S.]]

[[Category: Najmudin, S.]]

[[Category: Nalini, V.]]

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[[Category: eye lens protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 19:37:~~17 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:22 2008''

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@@ Line 1: / Line 1: @@
-[[Image:4gcr.jpg|left|200px]]<br /><applet load="4gcr" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:4gcr.jpg|left|200px]]<br /><applet load="4gcr" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="4gcr, resolution 1.47&Aring;" />
 '''STRUCTURE OF THE BOVINE EYE LENS PROTEIN GAMMA-B (GAMMA-II)-CRYSTALLIN AT 1.47 ANGSTROMS'''<br />
 ==Overview==
-The molecular structure of calf gammaB-crystallin (previously called, gammaII), a lens-specific protein, has been refined to a crystallographic, R factor of 18.1% for all reflection data, between 8.0 and 1.47 A, 25 959, hkl measured at 293 (1) K. 230 water molecules have been defined by, difference Fourier techniques and included in a restrained least-squares, refinement. Difference Fourier maps clearly indicated the presence of, multiple sites for the sulfur atoms of Cys 18 and Cys 22 which were, therefore given coupled second-site occupancies during the refinement. The, sulfur atom in the major position of Cys 22 is in the reduced state., Either of the Cys 18 sites can form a high-energy disulfide bridge with, the minor position of Cys 22. The position of the carboxy terminus and, many other surface side chains have been further defined including the RGD, signal peptide. The hydration of the backbone and the interdomain region, has been analysed. 27 water molecules make extensive contacts to a single, protein molecule and thus contribute to its stability.
+The molecular structure of calf gammaB-crystallin (previously called gammaII), a lens-specific protein, has been refined to a crystallographic R factor of 18.1% for all reflection data, between 8.0 and 1.47 A, 25 959 hkl measured at 293 (1) K. 230 water molecules have been defined by difference Fourier techniques and included in a restrained least-squares refinement. Difference Fourier maps clearly indicated the presence of multiple sites for the sulfur atoms of Cys 18 and Cys 22 which were therefore given coupled second-site occupancies during the refinement. The sulfur atom in the major position of Cys 22 is in the reduced state. Either of the Cys 18 sites can form a high-energy disulfide bridge with the minor position of Cys 22. The position of the carboxy terminus and many other surface side chains have been further defined including the RGD signal peptide. The hydration of the backbone and the interdomain region has been analysed. 27 water molecules make extensive contacts to a single protein molecule and thus contribute to its stability.
 ==About this Structure==
-GCR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure superseeds the now removed PDB entry 1GCR. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4GCR OCA].
+GCR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry 1GCR. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GCR OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Bos taurus]]
 [[Category: Single protein]]
-[[Category: Blundell, T.L.]]
+[[Category: Blundell, T L.]]
-[[Category: Driessen, H.P.C.]]
+[[Category: Driessen, H P.C.]]
 [[Category: Lindley, P.]]
-[[Category: Moss, D.S.]]
+[[Category: Moss, D S.]]
 [[Category: Najmudin, S.]]
 [[Category: Nalini, V.]]
@@ Line 22: / Line 22: @@
 [[Category: eye lens protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:37:17 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:22 2008''