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pubmed-article:1920418pubmed:dateCreated1991-10-25lld:pubmed
pubmed-article:1920418pubmed:abstractTextA recombinant form of human granulocyte-macrophage colony stimulating factor (GM-CSF) which contains no carbohydrate has been crystallized. Multiple isomorphous replacement analysis using five heavy-atom derivatives has yielded an image of the structure at 6 A resolution that showed two molecules per asymmetric unit and allowed determination of the non-crystallographic symmetry transformation. The 6 A resolution result shows that the core of GM-CSF consists of four helices. The angles at which the helices pack together distinguishes this structure from known antiparallel four-helix bundle proteins. Consideration of the amino acid sequence properties and previous structural characterizations of GM-CSF leads to an assignment of the probable protein segments that form the helices.lld:pubmed
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pubmed-article:1920418pubmed:issn0022-2836lld:pubmed
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pubmed-article:1920418pubmed:pagination55-60lld:pubmed
pubmed-article:1920418pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:1920418pubmed:year1991lld:pubmed
pubmed-article:1920418pubmed:articleTitleLow-resolution structure of recombinant human granulocyte-macrophage colony stimulating factor.lld:pubmed
pubmed-article:1920418pubmed:affiliationSection of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853.lld:pubmed
pubmed-article:1920418pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1920418pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
pubmed-article:1920418pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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