Amyloid fibrils are made up of a misfolded, self-assembled protein organised into a well-defined, repetitive structure. They are well known for their important role in protein misfolding diseases, including Alzheimer's disease and type 2 diabetes, in which the insoluble amyloid fibrils are deposited in the tissues. Furthermore, they have been found to play an important functional role in many organisms, providing strength, scaffolding, and protection. The first structural models of amyloid were informed by X-ray fiber diffraction data collection from bundles of aligned amyloid fibrils. This resulted in early models of the generic cross-β structure which has been superseded by more detailed diffraction analysis from highly oriented and semi-crystalline samples, resulting in details of the organization of peptides into a repetitive architecture. Here, we focused on describing methods of determining the underlying architecture of these fibrils, and we have described the common features of amyloid fibrils from diverse pathogenic, functional, and synthetic sources. We describe the preparation of the samples, data collection, and subsequent data analysis to produce a model structure that can be compared to the experimental data.