| pubmed-article:7615087 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7615087 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:7615087 | lifeskim:mentions | umls-concept:C1522642 | lld:lifeskim |
| pubmed-article:7615087 | lifeskim:mentions | umls-concept:C0332255 | lld:lifeskim |
| pubmed-article:7615087 | lifeskim:mentions | umls-concept:C0059040 | lld:lifeskim |
| pubmed-article:7615087 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
| pubmed-article:7615087 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:7615087 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:7615087 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:7615087 | pubmed:dateCreated | 1995-8-24 | lld:pubmed |
| pubmed-article:7615087 | pubmed:abstractText | A 25 kDa C-terminal tryptic fragment of elongation factor Ts has been purified to homogeneity. Experimental evidence suggests that the 25 kDa C-terminal and the 5.3 kDa N-terminal fragments are structurally independent domains. The N-terminal fragment is shown to be essential for the nucleotide exchange activity. Crystals of the C-terminal fragment belong to space group P2 or P2(1). The diffraction pattern shows a pronounced pseudo-C2 symmetry at low resolution. This pseudo symmetry increases when the crystals are irradiated with X-rays for a few hours. | lld:pubmed |
| pubmed-article:7615087 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7615087 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7615087 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7615087 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7615087 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7615087 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7615087 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7615087 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7615087 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7615087 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7615087 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:7615087 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:7615087 | pubmed:author | pubmed-author:NyborgJJ | lld:pubmed |
| pubmed-article:7615087 | pubmed:author | pubmed-author:WiborgOO | lld:pubmed |
| pubmed-article:7615087 | pubmed:author | pubmed-author:ThirupSS | lld:pubmed |
| pubmed-article:7615087 | pubmed:author | pubmed-author:BøgestrandSS | lld:pubmed |
| pubmed-article:7615087 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7615087 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:7615087 | pubmed:volume | 368 | lld:pubmed |
| pubmed-article:7615087 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7615087 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7615087 | pubmed:pagination | 49-54 | lld:pubmed |
| pubmed-article:7615087 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7615087 | pubmed:meshHeading | pubmed-meshheading:7615087-... | lld:pubmed |
| pubmed-article:7615087 | pubmed:meshHeading | pubmed-meshheading:7615087-... | lld:pubmed |
| pubmed-article:7615087 | pubmed:meshHeading | pubmed-meshheading:7615087-... | lld:pubmed |
| pubmed-article:7615087 | pubmed:meshHeading | pubmed-meshheading:7615087-... | lld:pubmed |
| pubmed-article:7615087 | pubmed:meshHeading | pubmed-meshheading:7615087-... | lld:pubmed |
| pubmed-article:7615087 | pubmed:meshHeading | pubmed-meshheading:7615087-... | lld:pubmed |
| pubmed-article:7615087 | pubmed:meshHeading | pubmed-meshheading:7615087-... | lld:pubmed |
| pubmed-article:7615087 | pubmed:meshHeading | pubmed-meshheading:7615087-... | lld:pubmed |
| pubmed-article:7615087 | pubmed:meshHeading | pubmed-meshheading:7615087-... | lld:pubmed |
| pubmed-article:7615087 | pubmed:meshHeading | pubmed-meshheading:7615087-... | lld:pubmed |
| pubmed-article:7615087 | pubmed:meshHeading | pubmed-meshheading:7615087-... | lld:pubmed |
| pubmed-article:7615087 | pubmed:meshHeading | pubmed-meshheading:7615087-... | lld:pubmed |
| pubmed-article:7615087 | pubmed:meshHeading | pubmed-meshheading:7615087-... | lld:pubmed |
| pubmed-article:7615087 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7615087 | pubmed:articleTitle | Analysis and crystallization of a 25 kDa C-terminal fragment of cloned elongation factor Ts from Escherichia coli. | lld:pubmed |
| pubmed-article:7615087 | pubmed:affiliation | Department of Chemistry, Aarhus University, Denmark. | lld:pubmed |
| pubmed-article:7615087 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7615087 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:944866 | entrezgene:pubmed | pubmed-article:7615087 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7615087 | lld:pubmed |
