1540688

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0010423, umls-concept:C0023779, umls-concept:C0025252, umls-concept:C0348080, umls-concept:C0521009, umls-concept:C1622418, umls-concept:C2587213
pubmed:issue	1
pubmed:dateCreated	1992-4-3
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.
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0370626
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Dimyristoylphosphatidylcholine, http://linkedlifedata.com/resource/pubmed/chemical/Liposomes
pubmed:status	MEDLINE
pubmed:month	Jan
pubmed:issn	0006-3495
pubmed:author	pubmed-author:BaumeisterWW, pubmed-author:EngelhardtHH, pubmed-author:JakubowskiUU, pubmed-author:PaulAA
pubmed:issnType	Print
pubmed:volume	61
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	172-88
pubmed:dateRevised	2010-9-7
pubmed:meshHeading	pubmed-meshheading:1540688-Bacterial Outer Membrane Proteins, pubmed-meshheading:1540688-Crystallization, pubmed-meshheading:1540688-Dimyristoylphosphatidylcholine, pubmed-meshheading:1540688-Light, pubmed-meshheading:1540688-Liposomes, pubmed-meshheading:1540688-Microscopy, Electron, pubmed-meshheading:1540688-Models, Structural, pubmed-meshheading:1540688-Protein Conformation, pubmed-meshheading:1540688-Pseudomonas, pubmed-meshheading:1540688-Scattering, Radiation, pubmed-meshheading:1540688-Thermodynamics
pubmed:year	1992
pubmed:articleTitle	Two-dimensional crystallization of a bacterial surface protein on lipid vesicles under controlled conditions.
pubmed:affiliation	Max-Planck-Institut für Biochemie, Martinsried, Germany.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't