title: Preparation of Crystalline Samples of Amyloid Fibrils and Oligomers.
abstract: 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 full-length 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.
authors.affiliation: Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
authors.forename: Asher
authors.initials: A
authors.lastname: Moshe
authors.affiliation: Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
authors.forename: Meytal
authors.initials: M
authors.lastname: Landau
authors.affiliation: Department of Biological Chemistry, Howard Hughes Medical Institute (HHMI), University of California Los Angeles (UCLA), 611 Charles Young Dr. East, Los Angeles, CA, 90095-1569, USA. david@mbi.ucla.edu.
authors.forename: David
authors.initials: D
authors.lastname: Eisenberg
mesh_terms: D000595:Amino Acid Sequence / Q000235:genetics; D000682:Amyloid / Q000737:chemistry* / Q000648:ultrastructure; D058227:Amyloidogenic Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D055503:Protein Multimerization / Q000235:genetics
chemical_list: D000682:Amyloid; D058227:Amyloidogenic Proteins; D010446:Peptide Fragments
keywords: Amyloid-like peptides; Cross-β spine; Cylindrin; Microcrystallography; Microcrystals; Steric zipper