1vln: Difference between revisions
New page: left|200px<br /><applet load="1vln" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vln, resolution 2.4Å" /> '''A TRICLINIC CRYSTAL F... |
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[[Image:1vln.jpg|left|200px]]<br /><applet load="1vln" size=" | [[Image:1vln.jpg|left|200px]]<br /><applet load="1vln" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1vln, resolution 2.4Å" /> | caption="1vln, resolution 2.4Å" /> | ||
'''A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A'''<br /> | '''A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A'''<br /> | ||
==Overview== | ==Overview== | ||
The molecular structure of a triclinic crystal form of concanavalin A has | 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== | ==About this Structure== | ||
1VLN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1VLN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLN OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Canavalia ensiformis]] | [[Category: Canavalia ensiformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hamodrakas, S | [[Category: Hamodrakas, S J.]] | ||
[[Category: Kanellopoulos, P | [[Category: Kanellopoulos, P N.]] | ||
[[Category: Tucker, P | [[Category: Tucker, P A.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: manganese]] | [[Category: manganese]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:38 2008'' | ||
Revision as of 16:36, 21 February 2008
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A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A
OverviewOverview
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 StructureAbout this Structure
1VLN is a Single protein structure of sequence from Canavalia ensiformis with and as ligands. 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 Thu Feb 21 15:36:38 2008