2sar: Difference between revisions

Revision as of 15:52, 27 July 2008

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File:2sar.png

Template:STRUCTURE 2sar

DETERMINATION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURES OF RIBONUCLEASE SA AND ITS COMPLEX WITH 3'-GUANYLIC ACID AT 1.8 ANGSTROMS RESOLUTIONDETERMINATION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURES OF RIBONUCLEASE SA AND ITS COMPLEX WITH 3'-GUANYLIC ACID AT 1.8 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1654932

About this StructureAbout this Structure

2SAR is a Single protein structure of sequence from Streptomyces aureofaciens. Full crystallographic information is available from OCA.

ReferenceReference

Determination and restrained least-squares refinement of the structures of ribonuclease Sa and its complex with 3'-guanylic acid at 1.8 A resolution., Sevcik J, Dodson EJ, Dodson GG, Acta Crystallogr B. 1991 Apr 1;47 ( Pt 2):240-53. PMID:1654932

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2sar|  PDB=2sar  |  SCENE=  }}
-'''DETERMINATION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURES OF RIBONUCLEASE SA AND ITS COMPLEX WITH 3'-GUANYLIC ACID AT 1.8 ANGSTROMS RESOLUTION'''
+===DETERMINATION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURES OF RIBONUCLEASE SA AND ITS COMPLEX WITH 3'-GUANYLIC ACID AT 1.8 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The crystal structures of ribonuclease from Streptomyces aureofaciens (RNase Sa) and its complex with 3'-guanylic acid (guanosine 3'-monophosphate, 3'-GMP) have been determined by the method of isomorphous replacement. The atomic parameters have been refined by restrained least-squares minimization using data in the resolution range 10.0-1.8 A. All protein atoms and more than 230 water atoms in the two crystal structures have been refined to crystallographic R factors of 0.172 and 0.175 respectively. The estimated r.m.s. error in the atomic positions ranges from 0.2 A for well-defined atoms to about 0.5 A for more poorly defined atoms. There are two enzyme molecules in the asymmetric unit, built independently, and referred to as molecules A and B. The value of the average B factor for protein atoms in both structures is about 19 A2 and for water molecules about 35 A2. Electron density for the substrate analogue 3'-GMP was found only at the active site of molecule A. The density was very clear and the positions of all 3'-GMP atoms were refined with precision comparable to that of the protein.
+The line below this paragraph, {{ABSTRACT_PUBMED_1654932}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1654932 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_1654932}}
 ==About this Structure==
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 [[Category: Dodson, G G.]]
 [[Category: Sevcik, J.]]
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