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000904314 1001_ $$0P:(DE-Juel1)176935$$aZielinski, Mara$$b0
000904314 245__ $$aChallenges in sample preparation and structure determination of amyloids by cryo-EM
000904314 260__ $$aBethesda, Md.$$bSoc.$$c2021
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000904314 520__ $$aAmyloids 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.
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000904314 7001_ $$0P:(DE-Juel1)174309$$aRöder, Christine$$b1
000904314 7001_ $$0P:(DE-Juel1)132018$$aSchröder, Gunnar F.$$b2$$eCorresponding author
000904314 773__ $$0PERI:(DE-600)1474604-9$$a10.1016/j.jbc.2021.100938$$gVol. 297, no. 2, p. 100938 -$$n2$$p100938 -$$tThe journal of biological chemistry$$v297$$x0021-9258$$y2021
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