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@ARTICLE{Zielinski:904314,
author = {Zielinski, Mara and Röder, Christine and Schröder, Gunnar
F.},
title = {{C}hallenges in sample preparation and structure
determination of amyloids by cryo-{EM}},
journal = {The journal of biological chemistry},
volume = {297},
number = {2},
issn = {0021-9258},
address = {Bethesda, Md.},
publisher = {Soc.},
reportid = {FZJ-2021-05884},
pages = {100938 -},
year = {2021},
abstract = {Amyloids share a common architecture but play disparate
biological roles in processes ranging from bacterial defense
mechanisms to protein misfolding diseases. Their structures
are highly polymorphic, which makes them difficult to study
by X-ray diffraction or NMR spectroscopy. Our understanding
of amyloid structures is due in large part to recent
advances in the field of cryo-EM, which allows for
determining the polymorphs separately. In this review, we
highlight the main stepping stones leading to the
substantial number of high-resolution amyloid fibril
structures known today as well as recent developments
regarding automation and software in cryo-EM. We discuss
that sample preparation should move closer to physiological
conditions to understand how amyloid aggregation and disease
are linked. We further highlight new approaches to address
heterogeneity and polymorphism of amyloid fibrils in EM
image processing and give an outlook to the upcoming
challenges in researching the structural biology of
amyloids.},
cin = {IBI-7},
ddc = {540},
cid = {I:(DE-Juel1)IBI-7-20200312},
pnm = {5244 - Information Processing in Neuronal Networks
(POF4-524)},
pid = {G:(DE-HGF)POF4-5244},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:34224730},
UT = {WOS:000690871000008},
doi = {10.1016/j.jbc.2021.100938},
url = {https://juser.fz-juelich.de/record/904314},
}