| pubmed-article:15583400 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15583400 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:15583400 | lifeskim:mentions | umls-concept:C0021699 | lld:lifeskim |
| pubmed-article:15583400 | lifeskim:mentions | umls-concept:C0010424 | lld:lifeskim |
| pubmed-article:15583400 | pubmed:issue | Pt 12 Pt 2 | lld:pubmed |
| pubmed-article:15583400 | pubmed:dateCreated | 2004-12-7 | lld:pubmed |
| pubmed-article:15583400 | pubmed:abstractText | Crystals of the EmrE membrane-protein imposed several technical challenges for X-ray crystallography, including high mosaicity, poor diffraction and a relatively large number of heavy atoms. Consequently, the heavy-atom substructure solution was difficult to obtain. By removing the histidine tag for protein purification, the mosaicity and the diffraction quality were greatly improved. The direct-methods Shake-and-Bake program SnB was successful in locating the heavy-atom sites from a mutant of EmrE which lacks a cysteine and therefore has a reduction in the number of heavy-atom sites. The substructure solution was solved from data with anomalous difference at a resolution of 5.5 A and the structure was determined to 3.8 A. | lld:pubmed |
| pubmed-article:15583400 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15583400 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15583400 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15583400 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15583400 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15583400 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15583400 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15583400 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15583400 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15583400 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15583400 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15583400 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:15583400 | pubmed:issn | 0907-4449 | lld:pubmed |
| pubmed-article:15583400 | pubmed:author | pubmed-author:AliJJ | lld:pubmed |
| pubmed-article:15583400 | pubmed:author | pubmed-author:ChangGeoffrey... | lld:pubmed |
| pubmed-article:15583400 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15583400 | pubmed:volume | 60 | lld:pubmed |
| pubmed-article:15583400 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15583400 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15583400 | pubmed:pagination | 2399-402 | lld:pubmed |
| pubmed-article:15583400 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:15583400 | pubmed:meshHeading | pubmed-meshheading:15583400... | lld:pubmed |
| pubmed-article:15583400 | pubmed:meshHeading | pubmed-meshheading:15583400... | lld:pubmed |
| pubmed-article:15583400 | pubmed:meshHeading | pubmed-meshheading:15583400... | lld:pubmed |
| pubmed-article:15583400 | pubmed:meshHeading | pubmed-meshheading:15583400... | lld:pubmed |
| pubmed-article:15583400 | pubmed:meshHeading | pubmed-meshheading:15583400... | lld:pubmed |
| pubmed-article:15583400 | pubmed:meshHeading | pubmed-meshheading:15583400... | lld:pubmed |
| pubmed-article:15583400 | pubmed:meshHeading | pubmed-meshheading:15583400... | lld:pubmed |
| pubmed-article:15583400 | pubmed:meshHeading | pubmed-meshheading:15583400... | lld:pubmed |
| pubmed-article:15583400 | pubmed:meshHeading | pubmed-meshheading:15583400... | lld:pubmed |
| pubmed-article:15583400 | pubmed:meshHeading | pubmed-meshheading:15583400... | lld:pubmed |
| pubmed-article:15583400 | pubmed:meshHeading | pubmed-meshheading:15583400... | lld:pubmed |
| pubmed-article:15583400 | pubmed:meshHeading | pubmed-meshheading:15583400... | lld:pubmed |
| pubmed-article:15583400 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15583400 | pubmed:articleTitle | Crystallography of the integral membrane protein EmrE from Escherichia coli. | lld:pubmed |
| pubmed-article:15583400 | pubmed:affiliation | Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, CB-105, La Jolla, CA 92037, USA. | lld:pubmed |
| pubmed-article:15583400 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15583400 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15583400 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:15583400 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:948442 | entrezgene:pubmed | pubmed-article:15583400 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:15583400 | lld:entrezgene |
