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@ARTICLE{Galkin:186656,
author = {Galkin, Vitold E. and Orlova, Albina and Vos, Matthijn R.
and Schröder, Gunnar and Egelman, Edward H.},
title = {{N}ear-{A}tomic {R}esolution for {O}ne {S}tate of
{F}-{A}ctin},
journal = {Structure},
volume = {23},
number = {1},
issn = {0969-2126},
address = {London [u.a.]},
publisher = {Elsevier Science},
reportid = {FZJ-2015-00729},
pages = {173 - 182},
year = {2015},
abstract = {Actin functions as a helical polymer, F-actin, but attempts
to build an atomic model for this filament have been
hampered by the fact that the filament cannot be
crystallized and by structural heterogeneity. We have used a
direct electron detector, cryo-electron microscopy, and the
forces imposed on actin filaments in thin films to
reconstruct one state of the filament at 4.7 Å resolution,
which allows for building a reliable pseudo-atomic model of
F-actin. We also report a different state of the filament
where actin protomers adopt a conformation observed in the
crystal structure of the G-actin-profilin complex with an
open ATP-binding cleft. Comparison of the two structural
states provides insights into ATP-hydrolysis and filament
dynamics. The atomic model provides a framework for
understanding why every buried residue in actin has been
under intense selective pressure.},
cin = {ICS-6},
ddc = {570},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551)},
pid = {G:(DE-HGF)POF3-551},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000347469500021},
pubmed = {pmid:25533486},
doi = {10.1016/j.str.2014.11.006},
url = {https://juser.fz-juelich.de/record/186656},
}