@inbook{26f06de75ed742998e96dab320a9195f,
title = "Structural characterization of prefibrillar intermediates and amyloid fibrils by small-angle X-ray scattering",
abstract = "Structural investigation of the species present during protein fibrillation is of tremendous importance, yet complicated by the equilibrium between species of very different sizes and life-times. Small-angle X-ray scattering may be applied to solve this problem, providing both information about the process (number of species present and volume fractions of individual species) and low-resolution three-dimensional shape reconstructions of individual species. Here, we describe in detail the challenges associated with the approach, exemplified using data from fibrillating insulin or α-synuclein samples.",
author = "Langkilde, {Annette Eva} and Bente Vestergaard",
note = "Part 1: In vitro models and assays, chapter 10 ",
year = "2012",
doi = "10.1007/978-1-61779-551-0_10",
language = "English",
isbn = "978-1-61779-550-3",
volume = "849",
series = "Methods in Molecular Biology",
publisher = "Springer Science+Business Media",
pages = "137--155",
editor = "Sigurdsson, {Einar M} and Miguel Calero and Maria Gasset",
booktitle = "Amyloid proteins",
address = "Singapore",
edition = "2",
}