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pubmed-article:1540688pubmed:abstractTextThe 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:1540688pubmed:authorpubmed-author:PaulAAlld:pubmed
pubmed-article:1540688pubmed:authorpubmed-author:EngelhardtHHlld:pubmed
pubmed-article:1540688pubmed:authorpubmed-author:BaumeisterWWlld:pubmed
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pubmed-article:1540688pubmed:pagination172-88lld:pubmed
pubmed-article:1540688pubmed:dateRevised2010-9-7lld:pubmed
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pubmed-article:1540688pubmed:articleTitleTwo-dimensional crystallization of a bacterial surface protein on lipid vesicles under controlled conditions.lld:pubmed
pubmed-article:1540688pubmed:affiliationMax-Planck-Institut für Biochemie, Martinsried, Germany.lld:pubmed
pubmed-article:1540688pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1540688pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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