rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1998-11-20
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pubmed:abstractText |
Oligomers of the chaperonin TF55 from Sulfolobus solfataricus have been successfully crystallized in two dimensions via their interaction with a phospholipid monolayer at the air/liquid interface. Oligomer orientation was dependent upon the lipid headgroup used. A neutral lipid monolayer gave rise to small paracrystalline areas of TF55 side views, whereas a negatively charged lipid monolayer resulted in large coherent crystalline areas of the chaperonin in an end-on orientation. These 2D crystals had p312 symmetry (a = b = 162 A, gamma = 60 degrees). Two-dimensional projection structures of the end-on arrays were produced by electron microscopy and image processing techniques. Under the conditions used to grow the crystals, the protein formed complexes of two stacked nine-subunit rings with threefold symmetry.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
|
pubmed:issn |
1047-8477
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 1998 Academic Press.
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pubmed:issnType |
Print
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pubmed:volume |
123
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30-6
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pubmed:dateRevised |
2009-7-17
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pubmed:meshHeading |
pubmed-meshheading:9774542-Archaeal Proteins,
pubmed-meshheading:9774542-Crystallization,
pubmed-meshheading:9774542-Dimyristoylphosphatidylcholine,
pubmed-meshheading:9774542-Heat-Shock Proteins,
pubmed-meshheading:9774542-Image Processing, Computer-Assisted,
pubmed-meshheading:9774542-Microscopy, Electron,
pubmed-meshheading:9774542-Molecular Chaperones,
pubmed-meshheading:9774542-Phosphatidylglycerols,
pubmed-meshheading:9774542-Protein Conformation,
pubmed-meshheading:9774542-Sulfolobus
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pubmed:year |
1998
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pubmed:articleTitle |
Two-dimensional crystallization of the chaperonin TF55 from the hyperthermophilic archaeon Sulfolobus solfataricus.
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pubmed:affiliation |
Department of Biosciences, Karolinska Institutet, Huddinge, S-141 57, Sweden. matthew@csb.ki.se
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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