Preparation of crystalline samples of amyloid fibrils and oligomers

Asher Moshe, Meytal Landau, David Eisenberg

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review


The molecular structures of amyloid fibers and oligomers are required in order to understand and control their formation. Yet, their partially disordered and polymorphic nature hinders structural analyses. Fortunately, short segments from amyloid proteins, which exhibit similar biophysical properties to the fulllength proteins, also form fibrils and oligomers and their atomic structures can be determined. Here we describe experimental procedures used to assess fiber-forming capabilities of amyloid peptide segments and their crystallization.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Number of pages10
StatePublished - 2016

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • Amyloid-like peptides
  • Cross-β spine
  • Cylindrin
  • Microcrystallography
  • Microcrystals
  • Steric zipper


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