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pubmed-article:18082422pubmed:abstractTextThere is a need for improved tools for labeling protein species within large macromolecular assemblies. Here we describe a method for the efficient selenomethionine labeling of the membrane-containing bacterial virus PM2 for structural studies. By examining potential host cells a strain was found which was auxotrophic for methionine, and by performing a multiparameter search of conditions it was possible to derive a robust protocol which simultaneously minimized the toxic effects of the selenomethionine, so that a reasonable virus yield was maintained, whilst still achieving essentially complete labeling. This has allowed us to fingerprint the protein constituents of the virus in a relatively low resolution electron density map. Such a technique can be adapted to other macromolecule complexes studied by X-ray crystallography.lld:pubmed
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pubmed-article:18082422pubmed:authorpubmed-author:BamfordJaana...lld:pubmed
pubmed-article:18082422pubmed:authorpubmed-author:StuartDavid...lld:pubmed
pubmed-article:18082422pubmed:authorpubmed-author:AbresciaNicol...lld:pubmed
pubmed-article:18082422pubmed:authorpubmed-author:KiveläHanna...lld:pubmed
pubmed-article:18082422pubmed:authorpubmed-author:GrimesJonatha...lld:pubmed
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pubmed-article:18082422pubmed:volume161lld:pubmed
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pubmed-article:18082422pubmed:pagination204-10lld:pubmed
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pubmed-article:18082422pubmed:year2008lld:pubmed
pubmed-article:18082422pubmed:articleTitleSelenomethionine labeling of large biological macromolecular complexes: probing the structure of marine bacterial virus PM2.lld:pubmed
pubmed-article:18082422pubmed:affiliationDepartment of Biological and Environmental Science and Nanoscience Centre, University of Jyväskylä, P.O. Box 35 (Survontie 9), 40014 Jyväskylä, Finland.lld:pubmed
pubmed-article:18082422pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18082422pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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