| pubmed-article:8319804 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8319804 | lifeskim:mentions | umls-concept:C0085475 | lld:lifeskim |
| pubmed-article:8319804 | lifeskim:mentions | umls-concept:C0004022 | lld:lifeskim |
| pubmed-article:8319804 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:8319804 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
| pubmed-article:8319804 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8319804 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8319804 | pubmed:dateCreated | 1993-8-5 | lld:pubmed |
| pubmed-article:8319804 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8319804 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8319804 | pubmed:abstractText | The genes of aspartyl-tRNA synthetase (AspRS) from two Thermus thermophilus strain VK-1 and HB8, have been cloned and sequenced. Their nucleotidic sequences code for the same protein which displays the three characteristic motifs of class II aminoacyl-tRNA synthetases. This enzyme shows 50% identity with Escherichia coli AspRS, over the totality of the chain (580 amino acids). A comparison with the eukaryotic yeast cytoplasmic AspRS indicates the presence in the prokaryotic AspRS of an extra domain between motifs 2 and 3 much larger than in the eukaryotic ones. When its gene is under the control of the tac promoter of the expression vector pKK223-3, the protein is efficiently overexpressed as a thermostable protein in E. coli. It can be further purified to homogeneity using a heat treatment followed by a single anion exchange chromatography. Single crystals of the pure protein, diffracting at least to 2.2 A resolution (space group P2(1)2(1)2(1), a = 61.4 A, b = 156.1 A, c = 177.3 A) are routinely obtained. The same crystals have previously been described as crystals of threonyl-tRNA synthetase [1]. | lld:pubmed |
| pubmed-article:8319804 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8319804 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8319804 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8319804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8319804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8319804 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8319804 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:8319804 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:8319804 | pubmed:author | pubmed-author:KerrHH | lld:pubmed |
| pubmed-article:8319804 | pubmed:author | pubmed-author:BlanquetSS | lld:pubmed |
| pubmed-article:8319804 | pubmed:author | pubmed-author:MorayNN | lld:pubmed |
| pubmed-article:8319804 | pubmed:author | pubmed-author:KreutzerRR | lld:pubmed |
| pubmed-article:8319804 | pubmed:author | pubmed-author:PlateauPP | lld:pubmed |
| pubmed-article:8319804 | pubmed:author | pubmed-author:PoterszmanAA | lld:pubmed |
| pubmed-article:8319804 | pubmed:author | pubmed-author:MazauricM HMH | lld:pubmed |
| pubmed-article:8319804 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8319804 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:8319804 | pubmed:volume | 325 | lld:pubmed |
| pubmed-article:8319804 | pubmed:geneSymbol | aspS | lld:pubmed |
| pubmed-article:8319804 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8319804 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8319804 | pubmed:pagination | 183-6 | lld:pubmed |
| pubmed-article:8319804 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8319804 | pubmed:meshHeading | pubmed-meshheading:8319804-... | lld:pubmed |
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| pubmed-article:8319804 | pubmed:meshHeading | pubmed-meshheading:8319804-... | lld:pubmed |
| pubmed-article:8319804 | pubmed:meshHeading | pubmed-meshheading:8319804-... | lld:pubmed |
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| pubmed-article:8319804 | pubmed:meshHeading | pubmed-meshheading:8319804-... | lld:pubmed |
| pubmed-article:8319804 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8319804 | pubmed:articleTitle | Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases. | lld:pubmed |
| pubmed-article:8319804 | pubmed:affiliation | Laboratoire de Biochimie, URA 240 CNRS, Ecole Polytechnique, Palaiseau, France. | lld:pubmed |
| pubmed-article:8319804 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8319804 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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