1vln

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{{STRUCTURE_1vln| PDB=1vln | SCENE= }}
{{STRUCTURE_1vln| PDB=1vln | SCENE= }}
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'''A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A'''
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===A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A===
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==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.
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The line below this paragraph, {{ABSTRACT_PUBMED_8812975}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 8812975 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8812975}}
==About this Structure==
==About this Structure==
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[[Category: Legume]]
[[Category: Legume]]
[[Category: Manganese]]
[[Category: Manganese]]
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Revision as of 05:08, 29 July 2008

Template:STRUCTURE 1vln

A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A

Template:ABSTRACT PUBMED 8812975

About this Structure

1VLN is a Single protein structure of sequence from Canavalia ensiformis. 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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