| pubmed-article:3309338 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3309338 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:3309338 | lifeskim:mentions | umls-concept:C1419686 | lld:lifeskim |
| pubmed-article:3309338 | lifeskim:mentions | umls-concept:C1539707 | lld:lifeskim |
| pubmed-article:3309338 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:3309338 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:3309338 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:3309338 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:3309338 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:3309338 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:3309338 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:3309338 | pubmed:dateCreated | 1987-11-12 | lld:pubmed |
| pubmed-article:3309338 | pubmed:abstractText | The structure of a C-terminal fragment of the ribosomal protein L7/L12 from Escherichia coli has been refined using crystallographic data to 1.7 A resolution. The R-value is 17.4%. Six residues at the N terminus are too disordered in the structure to be localized. These residues are probably part of a hinge in the complete L7/L12 molecule. The possibility that a 2-fold crystallographic axis is a molecular 2-fold axis is discussed. A patch of invariant residues on the surface of the dimer is probably involved in functional interactions with elongation factors. | lld:pubmed |
| pubmed-article:3309338 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3309338 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3309338 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3309338 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3309338 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:3309338 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:3309338 | pubmed:author | pubmed-author:LiljasAA | lld:pubmed |
| pubmed-article:3309338 | pubmed:author | pubmed-author:LeijonmarckMM | lld:pubmed |
| pubmed-article:3309338 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3309338 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:3309338 | pubmed:volume | 195 | lld:pubmed |
| pubmed-article:3309338 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3309338 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3309338 | pubmed:pagination | 555-79 | lld:pubmed |
| pubmed-article:3309338 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:3309338 | pubmed:meshHeading | pubmed-meshheading:3309338-... | lld:pubmed |
| pubmed-article:3309338 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3309338 | pubmed:articleTitle | Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A. | lld:pubmed |
| pubmed-article:3309338 | pubmed:affiliation | Institute of Molecular Biology, University of Uppsala, Sweden. | lld:pubmed |
| pubmed-article:3309338 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3309338 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:948489 | entrezgene:pubmed | pubmed-article:3309338 | lld:entrezgene |
| family:PF00542.14 | family:pubmed | pubmed-article:3309338 | lld:pfam |
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