1vln

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(New page: 200px<br /><applet load="1vln" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vln, resolution 2.4&Aring;" /> '''A TRICLINIC CRYSTAL F...)
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Revision as of 02:49, 21 November 2007

Image:1vln.jpg

1vln, resolution 2.4Å

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A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A

Overview

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.

About this Structure

1VLN is a Single protein structure of sequence from Canavalia ensiformis with MN and CA as ligands. Full crystallographic information is available from OCA.

Reference

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

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