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X-Ray Fibre Diffraction Studies of Amyloid Fibrils

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Amyloid Proteins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 849))

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.

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Author information

Authors and Affiliations

  1. School of Life Sciences, University of Sussex, Brighton, UK

    Kyle L. Morris & Louise C. Serpell

Authors
  1. Kyle L. Morris
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  2. Louise C. Serpell
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Corresponding author

Correspondence to Louise C. Serpell .

Editor information

Editors and Affiliations

  1. School of Medicine, Dept. Psychiatry, New York University, First Ave. 550, New York, 10016, New York, USA

    Einar M. Sigurdsson

  2. Centro Nacional de Microbiología, Instituto de Salud Carlos III, Carretera Majadahonda-Pozuelo Km 2, Madrid, 28220, Spain

    Miguel Calero

  3. Inst. Química Física, Rocasolano, CSIC Madrid, C/ Serrano 119, Madrid, 28006, Spain

    María Gasset

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Morris, K.L., Serpell, L.C. (2012). X-Ray Fibre Diffraction Studies of Amyloid Fibrils. In: Sigurdsson, E., Calero, M., Gasset, M. (eds) Amyloid Proteins. Methods in Molecular Biology, vol 849. Humana Press. https://doi.org/10.1007/978-1-61779-551-0_9

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  • DOI: https://doi.org/10.1007/978-1-61779-551-0_9

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  • Publisher Name: Humana Press

  • Print ISBN: 978-1-61779-550-3

  • Online ISBN: 978-1-61779-551-0

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