Determining Rg of IDPs from SAXS Data

Research output: Contribution to journalArticlepeer-review

Abstract

There is a great interest within the research community to understand the structure-function relationship for intrinsically disordered proteins (IDPs); however, the heterogeneous distribution of conformations that IDPs can adopt limits the applicability of conventional structural biology methods. Here, scattering techniques, such as small-angle X-ray scattering, can contribute. In this chapter, we will describe how to make a model-free determination of the radius of gyration by using two different approaches, the Guinier analysis and the pair distance distribution function. The ATSAS package (Franke et al., J Appl Crystallogr 50:1212-1225, 2017) has been used for the evaluation, and throughout the chapter, different examples will be given to illustrate the discussed phenomena, as well as the pros and cons of using the different approaches.

Original languageEnglish
Pages (from-to)271-283
Number of pages13
JournalMethods in molecular biology (Clifton, N.J.)
Volume2141
DOIs
Publication statusPublished - 2020

Subject classification (UKÄ)

  • Structural Biology

Keywords

  • ATSAS
  • Flexible proteins
  • GNOM
  • Guinier
  • Intrinsically disordered proteins
  • Pair distance distribution function
  • PRIMUS
  • Radius of gyration
  • Scattering

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