| pubmed-article:7536435 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7536435 | lifeskim:mentions | umls-concept:C0023779 | lld:lifeskim |
| pubmed-article:7536435 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:7536435 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
| pubmed-article:7536435 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:7536435 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:7536435 | lifeskim:mentions | umls-concept:C0121925 | lld:lifeskim |
| pubmed-article:7536435 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:7536435 | pubmed:dateCreated | 1995-5-24 | lld:pubmed |
| pubmed-article:7536435 | pubmed:abstractText | Recombinant proteins containing a short stretch of contiguous histidine residues (approximately 6) ("a His-tag") can be specifically bound to N-nitrilotriacetic-acid-chelated nickel ions, providing a convenient general method for their purification. A lipid derivatized with a nickel-chelating head group may provide a general approach to two-dimensional crystallization of the His-tagged proteins, using the lipid layer technique. We have designed a synthetic phospholipid that carries a chelated nickel ion (Ni-NTA-DOPE). His-tagged recombinant HIV-1 reverse transcriptase (HIV-RT) bound specifically to lipid layers containing Ni-NTA-DOPE and formed crystals within minutes from a dilute protein solution. Two-dimensional crystals preserved in negative stain diffracted strongly to approximately 21 A. The projection map computed from averaged Fourier transforms revealed a structure similar in size and shape to a selected projection view of the 3-D structure that was previously determined for HIV-RT by X-ray crystallography. | lld:pubmed |
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| pubmed-article:7536435 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7536435 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7536435 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7536435 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7536435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7536435 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7536435 | pubmed:issn | 1047-8477 | lld:pubmed |
| pubmed-article:7536435 | pubmed:author | pubmed-author:BrownP OPO | lld:pubmed |
| pubmed-article:7536435 | pubmed:author | pubmed-author:Le GriceS FSF | lld:pubmed |
| pubmed-article:7536435 | pubmed:author | pubmed-author:KubalekE WEW | lld:pubmed |
| pubmed-article:7536435 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7536435 | pubmed:volume | 113 | lld:pubmed |
| pubmed-article:7536435 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7536435 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7536435 | pubmed:pagination | 117-23 | lld:pubmed |
| pubmed-article:7536435 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:7536435 | pubmed:meshHeading | pubmed-meshheading:7536435-... | lld:pubmed |
| pubmed-article:7536435 | pubmed:meshHeading | pubmed-meshheading:7536435-... | lld:pubmed |
| pubmed-article:7536435 | pubmed:meshHeading | pubmed-meshheading:7536435-... | lld:pubmed |
| pubmed-article:7536435 | pubmed:meshHeading | pubmed-meshheading:7536435-... | lld:pubmed |
| pubmed-article:7536435 | pubmed:meshHeading | pubmed-meshheading:7536435-... | lld:pubmed |
| pubmed-article:7536435 | pubmed:meshHeading | pubmed-meshheading:7536435-... | lld:pubmed |
| pubmed-article:7536435 | pubmed:meshHeading | pubmed-meshheading:7536435-... | lld:pubmed |
| pubmed-article:7536435 | pubmed:meshHeading | pubmed-meshheading:7536435-... | lld:pubmed |
| pubmed-article:7536435 | pubmed:meshHeading | pubmed-meshheading:7536435-... | lld:pubmed |
| pubmed-article:7536435 | pubmed:articleTitle | Two-dimensional crystallization of histidine-tagged, HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid. | lld:pubmed |
| pubmed-article:7536435 | pubmed:affiliation | Howard Hughes Medical Institute, Stanford University, California. | lld:pubmed |
| pubmed-article:7536435 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7536435 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7536435 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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