* Corresponding authors

a Institute for Research in Biomedicine, Parc Científic de Barcelona, Baldiri Reixac, 10, 08028 Barcelona, Spain

b European Molecular Biology Laboratory, Hamburg Outstation, Notkestrasse 85, 22603 Hamburg, Germany
E-mail:pau.bernado@irbbarcelona.org,svergun@embl-hamburg.de

Abstract

Small-angle scattering of X-rays (SAXS) is an established method to study the overall structure and structural transitions of biologicalmacromolecules in solution. For foldedproteins, the technique provides three-dimensional low resolution structuresab initio or it can be used to drive rigid-body modeling.SAXS is also a powerful tool for the quantitative analysis of flexible systems, including intrinsically disorderedproteins (IDPs), and is highly complementary to the high resolution methods ofX-ray crystallography andNMR. Here we present the basic principles ofSAXS and review the main approaches to the characterization of IDPs and flexible multidomainproteins usingSAXS. Together with the standard approaches based on the analysis of overall parameters, a recently developed Ensemble Optimization Method (EOM) is now available. The latter method allows for the co-existence of multipleprotein conformations in solution compatible with the scattering data. Analysis of the selected ensembles provides quantitative information about flexibility and also offers insights into structural features. Examples of the use ofSAXS and combined approaches withNMR,X-ray crystallography, and computational methods to characterize completely or partially disorderedproteins are presented.

Graphical abstract: Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering

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Article information

Article type
Review Article
Submitted
04 Jul 2011
Accepted
02 Sep 2011
First published
22 Sep 2011

Mol. BioSyst., 2012,8, 151-167

Structural analysis of intrinsically disorderedproteins by small-angle X-ray scattering

P. Bernadó and D. I. Svergun,Mol. BioSyst., 2012, 8, 151DOI: 10.1039/C1MB05275F

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