| pubmed-article:15263845 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15263845 | lifeskim:mentions | umls-concept:C0034861 | lld:lifeskim |
| pubmed-article:15263845 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:15263845 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:15263845 | lifeskim:mentions | umls-concept:C0430054 | lld:lifeskim |
| pubmed-article:15263845 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:15263845 | lifeskim:mentions | umls-concept:C1705053 | lld:lifeskim |
| pubmed-article:15263845 | lifeskim:mentions | umls-concept:C2828366 | lld:lifeskim |
| pubmed-article:15263845 | lifeskim:mentions | umls-concept:C1705851 | lld:lifeskim |
| pubmed-article:15263845 | lifeskim:mentions | umls-concept:C1555707 | lld:lifeskim |
| pubmed-article:15263845 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:15263845 | lifeskim:mentions | umls-concept:C2752151 | lld:lifeskim |
| pubmed-article:15263845 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:15263845 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:15263845 | pubmed:dateCreated | 2004-7-20 | lld:pubmed |
| pubmed-article:15263845 | pubmed:abstractText | For structural and functional genomics programs, new high-throughput methods to characterize well-expressing and highly soluble proteins are essential. A faster and more convenient approach to screen expression conditions of recombinant proteins compared to classical in vivo systems is the Escherichia coli cell-free expression system. Here, we describe a rapid procedure to screen for expression and solubility of recombinant proteins using an E. coli cell-free extract. The results presented cover 24 open reading frames of unknown function from different micro-organisms. In order to screen different variables that may interfere with solubility, we expressed the recombinant proteins with a histidine6 tag, either N-terminal or C-terminal at two temperatures (25 degrees C and 30 degrees C). The identification of recombinant proteins is performed by the dot blot procedure using an anti-histidine tag antibody. We designed a rapid method that allows the characterization of soluble candidates from a large number of genes or from a large number of variants that is highly compatible with structural genomics expectations. | lld:pubmed |
| pubmed-article:15263845 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15263845 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15263845 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15263845 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15263845 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15263845 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15263845 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15263845 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15263845 | pubmed:issn | 1345-711X | lld:pubmed |
| pubmed-article:15263845 | pubmed:author | pubmed-author:KimSung-HouSH | lld:pubmed |
| pubmed-article:15263845 | pubmed:author | pubmed-author:KimRosalindR | lld:pubmed |
| pubmed-article:15263845 | pubmed:author | pubmed-author:BussoDidierD | lld:pubmed |
| pubmed-article:15263845 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15263845 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:15263845 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15263845 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15263845 | pubmed:pagination | 69-74 | lld:pubmed |
| pubmed-article:15263845 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:15263845 | pubmed:meshHeading | pubmed-meshheading:15263845... | lld:pubmed |
| pubmed-article:15263845 | pubmed:meshHeading | pubmed-meshheading:15263845... | lld:pubmed |
| pubmed-article:15263845 | pubmed:meshHeading | pubmed-meshheading:15263845... | lld:pubmed |
| pubmed-article:15263845 | pubmed:meshHeading | pubmed-meshheading:15263845... | lld:pubmed |
| pubmed-article:15263845 | pubmed:meshHeading | pubmed-meshheading:15263845... | lld:pubmed |
| pubmed-article:15263845 | pubmed:meshHeading | pubmed-meshheading:15263845... | lld:pubmed |
| pubmed-article:15263845 | pubmed:meshHeading | pubmed-meshheading:15263845... | lld:pubmed |
| pubmed-article:15263845 | pubmed:meshHeading | pubmed-meshheading:15263845... | lld:pubmed |
| pubmed-article:15263845 | pubmed:meshHeading | pubmed-meshheading:15263845... | lld:pubmed |
| pubmed-article:15263845 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15263845 | pubmed:articleTitle | Using an Escherichia coli cell-free extract to screen for soluble expression of recombinant proteins. | lld:pubmed |
| pubmed-article:15263845 | pubmed:affiliation | Department of Chemistry, University of California, Berkeley, CA 94720-5230, USA. | lld:pubmed |
| pubmed-article:15263845 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15263845 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15263845 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15263845 | lld:pubmed |
