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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
22
|
pubmed:dateCreated |
1982-1-28
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pubmed:abstractText |
Several individual intact ribosomal proteins purified from bacterial sources under mild conditions have been crystallized. A number of these are suitable candidates for three-dimensional structural studies by x-ray diffraction techniques. Data collection to 3 A resolution for one of these proteins is in progress.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
25
|
pubmed:volume |
256
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
11787-90
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7028741-Crystallization,
pubmed-meshheading:7028741-Escherichia coli,
pubmed-meshheading:7028741-Geobacillus stearothermophilus,
pubmed-meshheading:7028741-Protein Conformation,
pubmed-meshheading:7028741-Ribosomal Proteins,
pubmed-meshheading:7028741-Ribosomes,
pubmed-meshheading:7028741-X-Ray Diffraction
|
pubmed:year |
1981
|
pubmed:articleTitle |
The crystallization of ribosomal proteins from the 50 S subunit of the Escherichia coli and Bacillus stearothermophilus ribosome.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|