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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
|
pubmed:dateCreated |
1995-12-7
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pubmed:abstractText |
The ribosome--essential for protein synthesis in all organisms--has been an evasive target for structural studies. The best available structures for the 70S Escherichia coli ribosome or its 30S and 50S subunits are based on electron microscopical tilt experiments and are limited in resolution to 28-55 A. The angular reconstitution approach, which exploits the random orientations of particles within a vitreous ice matrix, can be used in conjunction with cryo-electron microscopy to yield a higher-resolution structure.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0969-2126
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
3
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
815-21
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7582898-Escherichia coli,
pubmed-meshheading:7582898-Freezing,
pubmed-meshheading:7582898-Microscopy, Electron,
pubmed-meshheading:7582898-Models, Structural,
pubmed-meshheading:7582898-RNA, Ribosomal,
pubmed-meshheading:7582898-Ribosomes,
pubmed-meshheading:7582898-X-Ray Diffraction
|
pubmed:year |
1995
|
pubmed:articleTitle |
The 70S Escherichia coli ribosome at 23 A resolution: fitting the ribosomal RNA.
|
pubmed:affiliation |
Fritz Haber Institute of the Max Planck Society, Berlin, Germany.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|