1caw: Difference between revisions

Revision as of 20:29, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1caw.png

Template:STRUCTURE 1caw

DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENTDETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT

Template:ABSTRACT PUBMED 15299507

About this StructureAbout this Structure

1CAW 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 Mon Jun 30 20:29:22 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1caw.jpg|left|200px]]
+{{Seed}}
+[[Image:1caw.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1caw|  PDB=1caw  |  SCENE=  }}
-'''DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT'''
+===DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15299507}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15299507 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15299507}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Ng, J D.]]
 [[Category: Seed storage protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:32:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:29:22 2008''