1qkd
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(New page: 200px<br /><applet load="1qkd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qkd, resolution 1.49Å" /> '''ERABUTOXIN'''<br /> ...)
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Revision as of 22:39, 20 November 2007
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ERABUTOXIN
Overview
Erabutoxin a has been crystallized in its monomeric and dimeric forms. The, structures were refined at 1.50 and 1.49 A resolution, respectively, using, synchrotron radiation data. The crystals belong to space group P212121, with cell dimensions a = 49.84, b = 46.62, c = 21.22 A for the monomer and, a = 55.32, b = 53.54, c = 40.76 A for the dimer. Using starting models, from earlier structure determinations, the monomeric structure refined to, an R value of 16.7% (8004 unique reflections, 17.0-1.50 A resolution, range), while the dimeric structure has been solved by the, molecular-replacement method with a final R value of 16.9% (19 444 unique, reflections, 17.4-1.49 A resolution range). The high-resolution, electron-density maps clearly revealed significant discrete disorder in, the proteins and allowed an accurate determination of the solvent, structure. For the monomer, the side chains of six residues were modelled, with alternate conformers and 106 sites for water molecules and one site, for a sulfate ion were included in the final model, whereas for the dimer, 206 sites for water molecules were included and both C-terminal residues, together with the side chains of 11 residues adopted alternative, conformations. A comparison was made with earlier structure, determinations. The features of the solvent structure of the erabutoxin, molecules are discussed in detail.
About this Structure
1QKD is a Single protein structure of sequence from Laticauda semifasciata. Full crystallographic information is available from OCA.
Reference
Structure of dimeric and monomeric erabutoxin a refined at 1.5 A resolution., Nastopoulos V, Kanellopoulos PN, Tsernoglou D, Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):964-74. PMID:9757111
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