title: X-ray fibre diffraction studies of amyloid fibrils.
abstract: Amyloid fibrils are polymeric assemblies of normally soluble proteins or peptides. To investigate their structure, it is generally not possible to use conventional methods of crystallography and solution nuclear magnetic resonance. To examine the repeating crystalline structure along the fibre axis, X-ray fibre diffraction has been a useful tool. Here we discuss the methods by which amyloid-like fibrils may be prepared to form a sample suitable for structural analysis and describe how data may be collected and then analysed to arrive at a potential model structure.
authors.affiliation: School of Life Sciences, University of Sussex, Brighton, UK.
authors.forename: Kyle L
authors.initials: KL
authors.lastname: Morris
authors.forename: Louise C
authors.initials: LC
authors.lastname: Serpell
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000302:isolation & purification; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000302:isolation & purification; D005898:Glass / Q000737:chemistry; D008854:Microscopy, Electron; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D017433:Protein Structure, Secondary; D012995:Solubility; D014961:X-Ray Diffraction / Q000295:instrumentation / Q000379:methods*
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42)