2rig: Difference between revisions

Revision as of 19:47, 21 February 2008

CRYSTAL STRUCTURE OF RECOMBINANT RABBIT INTERFERON-GAMMA AT 2.7-ANGSTROMS RESOLUTION

OverviewOverview

The crystal structure of recombinant rabbit interferon-gamma was solved by the multiple isomorphous replacement technique at 2.7-A resolution and refined to a crystallographic R-factor of 26.2%. The interferon crystallizes with one-half of the functional dimer in the asymmetric unit, with the two polypeptide chains of the dimer related by a crystallographic 2-fold symmetry axis. The structure is predominantly alpha-helical with extensive interdigitation of the alpha-helical segments of the two polypeptide chains.

About this StructureAbout this Structure

2RIG is a Single protein structure of sequence from Oryctolagus cuniculus. This structure supersedes the now removed PDB entry 1RIG. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of recombinant rabbit interferon-gamma at 2.7-A resolution., Samudzi CT, Burton LE, Rubin JR, J Biol Chem. 1991 Nov 15;266(32):21791-7. PMID:1939201

Page seeded by OCA on Thu Feb 21 18:47:42 2008

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OCA

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-[[Image:2rig.jpg|left|200px]]<br /><applet load="2rig" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2rig.jpg|left|200px]]<br /><applet load="2rig" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2rig, resolution 2.3&Aring;" />
 '''CRYSTAL STRUCTURE OF RECOMBINANT RABBIT INTERFERON-GAMMA AT 2.7-ANGSTROMS RESOLUTION'''<br />
 ==Overview==
-The crystal structure of recombinant rabbit interferon-gamma was solved by, the multiple isomorphous replacement technique at 2.7-A resolution and, refined to a crystallographic R-factor of 26.2%. The interferon, crystallizes with one-half of the functional dimer in the asymmetric unit, with the two polypeptide chains of the dimer related by a crystallographic, 2-fold symmetry axis. The structure is predominantly alpha-helical with, extensive interdigitation of the alpha-helical segments of the two, polypeptide chains.
+The crystal structure of recombinant rabbit interferon-gamma was solved by the multiple isomorphous replacement technique at 2.7-A resolution and refined to a crystallographic R-factor of 26.2%. The interferon crystallizes with one-half of the functional dimer in the asymmetric unit, with the two polypeptide chains of the dimer related by a crystallographic 2-fold symmetry axis. The structure is predominantly alpha-helical with extensive interdigitation of the alpha-helical segments of the two polypeptide chains.
 ==About this Structure==
-RIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. This structure superseeds the now removed PDB entry 1RIG. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2RIG OCA].
+RIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. This structure supersedes the now removed PDB entry 1RIG. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RIG OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Oryctolagus cuniculus]]
 [[Category: Single protein]]
-[[Category: Burton, L.E.]]
+[[Category: Burton, L E.]]
-[[Category: Rubin, J.R.]]
+[[Category: Rubin, J R.]]
-[[Category: Samudzi, C.T.]]
+[[Category: Samudzi, C T.]]
 [[Category: cytokine]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:57:36 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:47:42 2008''