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@ARTICLE{Polovinkin:185976,
author = {Polovinkin, V. and Gushchin, I. and Sintsov, M. and Round,
E. and Balandin, T. and Chervakov, P. and Shevchenko, Vitaly
and Utrobin, P. and Popov, A. and Borshchevskiy, V. and
Mishin, A. and Kuklin, A. and Willbold, D. and Chupin, V.
and Popot, J-L and Gordeliy, V.},
title = {{H}igh-resolution structure of a membrane protein
transferred from amphipol to a lipidic mesophase.},
journal = {The journal of membrane biology},
volume = {247},
number = {9-10},
issn = {1432-1424},
address = {New York, NY},
publisher = {Springer},
reportid = {FZJ-2015-00085},
pages = {997 - 1004},
year = {2014},
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.},
cin = {ICS-6},
ddc = {570},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {452 - Structural Biology (POF2-452)},
pid = {G:(DE-HGF)POF2-452},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:25192977},
UT = {WOS:000343835500019},
doi = {10.1007/s00232-014-9700-x},
url = {https://juser.fz-juelich.de/record/185976},
}