Form of presentation | Articles in Russian journals and collections |
Year of publication | 2014 |
Язык | английский |
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Sincov Mikhail Yurevich, author
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Polovinkin Vitaly -, author
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Bibliographic description in the original language |
Polovinkin V, High-resolution structure of a membrane protein transferred from amphipol to a lipidic mesophase. / Gushchin I, Sintsov M, Round E, Balandin T, Chervakov P, Schevchenko V, Utrobin P, Popov A, orshchevskiy V, Mishin A, Kuklin A, Willbold D,Chupin V, Popot JL, Gordeliy V. // J Membr Biol. 2014 Oct;247(9-10):997-1004. doi: 10.1007/s00232-014-9700-x. Epub 2014 Sep 6. |
Annotation |
Journal of Membrane Biology |
Keywords |
Amphipol, Membrane protein, crystallization, Bacteriorhodopsin, Monoolein, In meso crystallization |
The name of the journal |
Journal of Membrane Biology
|
URL |
http://link.springer.com/article/10.1007/s00232-014-9700-x/fulltext.html |
Please use this ID to quote from or refer to the card |
https://repository.kpfu.ru/eng/?p_id=124594&p_lang=2 |
Resource files | |
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Full metadata record |
Field DC |
Value |
Language |
dc.contributor.author |
Sincov Mikhail Yurevich |
ru_RU |
dc.contributor.author |
Polovinkin Vitaly - |
ru_RU |
dc.date.accessioned |
2014-01-01T00:00:00Z |
ru_RU |
dc.date.available |
2014-01-01T00:00:00Z |
ru_RU |
dc.date.issued |
2014 |
ru_RU |
dc.identifier.citation |
Polovinkin V, High-resolution structure of a membrane protein transferred from amphipol to a lipidic mesophase. / Gushchin I, Sintsov M, Round E, Balandin T, Chervakov P, Schevchenko V, Utrobin P, Popov A, orshchevskiy V, Mishin A, Kuklin A, Willbold D,Chupin V, Popot JL, Gordeliy V. // J Membr Biol. 2014 Oct;247(9-10):997-1004. doi: 10.1007/s00232-014-9700-x. Epub 2014 Sep 6. |
ru_RU |
dc.identifier.uri |
https://repository.kpfu.ru/eng/?p_id=124594&p_lang=2 |
ru_RU |
dc.description.abstract |
Journal of Membrane Biology |
ru_RU |
dc.description.abstract |
Journal of Membrane Biology |
ru_RU |
dc.description.abstract |
Amphipols (APols) have become important tools for the stabilization, folding, and in vitro structural and functional studies of membrane proteins (MPs). Direct crystallization of MPs solubilized in APols would be of high importance for structural biology. However, despite considerable efforts, it is still not clear whether MP/APol complexes can form well-ordered crystals suitable for X-ray crystallography. In the present work, we show that an APol-trapped MP can be crystallized in meso. Bacteriorhodopsin (BR) trapped by APol A8-35 was mixed with a lipidic mesophase, and crystallization was induced by adding a precipitant. The crystals diffract beyond 2 Å. The structure of BR was solved to 2 Å and found to be indistinguishable from previous structures obtained after transfer from detergent solutions. We suggest the proposed protocol of in meso crystallization to be generally applicable to APol-trapped MPs. |
ru_RU |
dc.language.iso |
ru |
ru_RU |
dc.subject |
Amphipol |
ru_RU |
dc.subject |
Membrane protein |
ru_RU |
dc.subject |
crystallization |
ru_RU |
dc.subject |
Bacteriorhodopsin |
ru_RU |
dc.subject |
Monoolein |
ru_RU |
dc.subject |
In meso crystallization |
ru_RU |
dc.title |
High-resolution structure of a membrane protein transferred from amphipol to a lipidic mesophase. |
ru_RU |
dc.type |
Articles in Russian journals and collections |
ru_RU |
|