DC Field | Value | Language |
---|---|---|
dc.contributor.author | Oh, Byung-Ha | ko |
dc.date.accessioned | 2013-03-03T07:08:16Z | - |
dc.date.available | 2013-03-03T07:08:16Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 1995-06 | - |
dc.identifier.citation | ACTA CRYSTALLOGRAPHICA - SECTION D BIOLOGICAL CRYSTALLOGRAPHY, v.51, no.2, pp.140 - 144 | - |
dc.identifier.issn | 0907-4449 | - |
dc.identifier.uri | http://hdl.handle.net/10203/77725 | - |
dc.description.abstract | It is often found in the crystallization of enzyme-inhibitor complexes that an inhibitor causes crystal packing which is different to that of native protein. This is the case for crystals of human non-pancreatic secreted phospholipase A(2) (124 residues) containing six molecules in the asymmetric unit when the protein is complexed with a potential acylamino analogue of a phospholid. The hexameric structure was determined by molecular replacement using the structure of monomeric native protein as a probe. As an extension to the experiment, it was tested whether a backbone polypeptide composed of 17% of a known monomeric structure could find its correct position on a target molecule in molecular replacement. A probe model composed of the backbone atoms of the N-terminal 77 residues of lysine-, arginine-, ornithine-binding protein (LAO, a total of 238 residues) liganded with lysine correctly finds its position on LAO liganded with histidine which crystallizes as a monomer in the asymmetric unit. The results indicate that as little as 17% of total diffracting matter can be used in molecular replacement to solve crystal structures or to obtain phase information which can be combined with phases obtained by the isomorphous-replacement method. | - |
dc.language | English | - |
dc.publisher | INTERNATIONAL UNION OF CRYSTALLOGRAPHY | - |
dc.subject | MULTIDOMAIN PROTEINS | - |
dc.subject | FRAGMENT | - |
dc.title | A PROBE MOLECULE COMPOSED OF 17-PERCENT OF TOTAL DIFFRACTING MATTER GIVES CORRECT SOLUTIONS IN MOLECULAR REPLACEMENT | - |
dc.type | Article | - |
dc.identifier.wosid | A1995QT47100003 | - |
dc.identifier.scopusid | 2-s2.0-0029132452 | - |
dc.type.rims | ART | - |
dc.citation.volume | 51 | - |
dc.citation.issue | 2 | - |
dc.citation.beginningpage | 140 | - |
dc.citation.endingpage | 144 | - |
dc.citation.publicationname | ACTA CRYSTALLOGRAPHICA - SECTION D BIOLOGICAL CRYSTALLOGRAPHY | - |
dc.identifier.doi | 10.1107/S0907444994010024 | - |
dc.contributor.localauthor | Oh, Byung-Ha | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | MULTIDOMAIN PROTEINS | - |
dc.subject.keywordPlus | FRAGMENT | - |
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