1cax: Difference between revisions
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[[Image:1cax.jpg|left|200px]] | [[Image:1cax.jpg|left|200px]] | ||
'''DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT''' | {{Structure | ||
|PDB= 1cax |SIZE=350|CAPTION= <scene name='initialview01'>1cax</scene>, resolution 2.6Å | |||
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'''DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CAX is a [ | 1CAX is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CAX OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15299507 15299507] | ||
[[Category: Canavalia ensiformis]] | [[Category: Canavalia ensiformis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: seed storage protein]] | [[Category: seed storage protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:22:06 2008'' | ||
Revision as of 11:22, 20 March 2008
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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
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