1cax: Difference between revisions

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[[Image:1cax.jpg|left|200px]]
[[Image:1cax.jpg|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cax OCA], [http://www.ebi.ac.uk/pdbsum/1cax PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cax RCSB]</span>
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'''DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT'''
'''DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT'''
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[[Category: McPherson, A.]]
[[Category: McPherson, A.]]
[[Category: Ng, J D.]]
[[Category: Ng, J D.]]
[[Category: seed storage protein]]
[[Category: Seed storage protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:32:05 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:18:08 2008''

Revision as of 12:32, 2 May 2008

File:1cax.jpg

Template:STRUCTURE 1cax

DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT


OverviewOverview

Canavalin, the major reserve protein of the jack bean, was obtained in four different crystal forms. From the structure determined by multiple isomorphous replacement in a hexagonal unit cell, the structures of three other crystals were determined by molecular replacement. In two cases, the rhombohedral and cubic crystals, placement was facilitated by coincidence of threefold molecular symmetry with crystallographic operators. In the orthorhombic crystal the canavalin trimer was the asymmetric unit. The rhombohedral, orthorhombic and cubic crystal structures were subsequently refined using a combination of several approaches with resulting R factors of 0.194, 0.185 and 0.211 at resolutions of 2.6, 2.6 and 2.3 A, respectively. Variation in the conformation of the molecule from crystal to crystal was small with an r.m.s. deviation in Calpha positions of 0.89 A. Packing is quite different among crystal forms but lattice interactions appear to play little role in the conformation of the molecule. Greatest variations in mean position are for those residues that also exhibit the greatest thermal motion. Crystal contacts in all crystals are mediated almost exclusively by hydrophilic side chains, and three to six intermolecular salt bridges per protein subunit are present in each case.

About this StructureAbout this Structure

1CAX is a Protein complex structure of sequences from Canavalia ensiformis. Full crystallographic information is available from OCA.

ReferenceReference

Determination of three crystal structures of canavalin by molecular replacement., Ko TP, Ng JD, Greenwood A, McPherson A, Acta Crystallogr D Biol Crystallogr. 1993 Sep 1;49(Pt 5):478-89. PMID:15299507 Page seeded by OCA on Fri May 2 12:32:05 2008

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