pubmed-article:1540688 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1540688 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
pubmed-article:1540688 | lifeskim:mentions | umls-concept:C0025252 | lld:lifeskim |
pubmed-article:1540688 | lifeskim:mentions | umls-concept:C1622418 | lld:lifeskim |
pubmed-article:1540688 | lifeskim:mentions | umls-concept:C0023779 | lld:lifeskim |
pubmed-article:1540688 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
pubmed-article:1540688 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
pubmed-article:1540688 | lifeskim:mentions | umls-concept:C0348080 | lld:lifeskim |
pubmed-article:1540688 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:1540688 | pubmed:dateCreated | 1992-4-3 | lld:pubmed |
pubmed-article:1540688 | pubmed:abstractText | The solubilized surface protein of the Gram-negative bacterium Comamonas acidovorans was reconstituted on lipid vesicles by means of controlled dialysis. To this end, a multichamber dialysis apparatus was built which allows one to control the temperature and the dialysis rate, to apply various temperatures or buffer systems and sample conditions in a single experiment, and to monitor the turbidity of the sample by means of light scattering. The reconstitution conditions were optimized such that the surface protein formed two-dimensional crystals suitable for electron crystallography. The recrystallized surface protein arrays gave a resolution of approximately 1.3 nm in projection after correlation averaging of negatively stained preparations. The surface protein assembled into partially self-contained two-dimensional crystals which possess a strong shape-determining effect and formed cylinders and various cone-shaped vesicles. The development of the various vesicle forms is described in a model. | lld:pubmed |
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pubmed-article:1540688 | pubmed:language | eng | lld:pubmed |
pubmed-article:1540688 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1540688 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1540688 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1540688 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1540688 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1540688 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1540688 | pubmed:month | Jan | lld:pubmed |
pubmed-article:1540688 | pubmed:issn | 0006-3495 | lld:pubmed |
pubmed-article:1540688 | pubmed:author | pubmed-author:PaulAA | lld:pubmed |
pubmed-article:1540688 | pubmed:author | pubmed-author:EngelhardtHH | lld:pubmed |
pubmed-article:1540688 | pubmed:author | pubmed-author:BaumeisterWW | lld:pubmed |
pubmed-article:1540688 | pubmed:author | pubmed-author:JakubowskiUU | lld:pubmed |
pubmed-article:1540688 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1540688 | pubmed:volume | 61 | lld:pubmed |
pubmed-article:1540688 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1540688 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1540688 | pubmed:pagination | 172-88 | lld:pubmed |
pubmed-article:1540688 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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pubmed-article:1540688 | pubmed:meshHeading | pubmed-meshheading:1540688-... | lld:pubmed |
pubmed-article:1540688 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1540688 | pubmed:articleTitle | Two-dimensional crystallization of a bacterial surface protein on lipid vesicles under controlled conditions. | lld:pubmed |
pubmed-article:1540688 | pubmed:affiliation | Max-Planck-Institut für Biochemie, Martinsried, Germany. | lld:pubmed |
pubmed-article:1540688 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1540688 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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