1vln: Difference between revisions

Revision as of 08:08, 29 July 2008

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File:1vln.png

Template:STRUCTURE 1vln

A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN AA TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A

Template:ABSTRACT PUBMED 8812975

About this StructureAbout this Structure

1VLN is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.

ReferenceReference

A Triclinic Crystal Form of the Lectin Concanavalin A, Kanellopoulos PN, Tucker PA, Pavlou K, Agianian B, Hamodrakas SJ, J Struct Biol. 1996 Jul;117(1):16-23. PMID:8812975

Page seeded by OCA on Tue Jul 29 08:08:13 2008

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OCA

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-'''A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A'''
+===A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A===
-==Overview==
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-The molecular structure of a triclinic crystal form of concanavalin A has been refined at 2.4 A resolution. The crystals have unit cell dimensions a = 78.8 A, b = 79.3 A, c = 133.3 A, alpha = 97.1degrees, beta = 90.2degrees, and gamma = 97.5degrees and contain two tetramers per asymmetric unit each with approximate 222 symmetry. The final crystallographic R-factor is 0.205 and the free-R-factor is 0.265 in the resolution range 6.0 to 2.4 A. The conformation of the tetramer is more similar to that found in concanavalin A saccharide complexes than in the previously reported I222 crystal form of uncomplexed concanavalin A. A comparison of the molecular packing between the two crystal forms shows a more open arrangement with large solvent channels through the crystal.
+The line below this paragraph, {{ABSTRACT_PUBMED_8812975}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_8812975}}
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