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Accurate assessment of mass, models and resolution by small-angle scattering

Author

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  • Robert P. Rambo

    (Advanced Light Source, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA)

  • John A. Tainer

    (Advanced Light Source, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA
    The Skaggs Institute for Chemical Biology, The Scripps Research Institute)

Abstract

Modern small-angle scattering (SAS) experiments with X-rays or neutrons provide a comprehensive, resolution-limited observation of the thermodynamic state. However, methods for evaluating mass and validating SAS-based models and resolution have been inadequate. Here we define the volume of correlation, Vc, a SAS invariant derived from the scattered intensities that is specific to the structural state of the particle, but independent of concentration and the requirements of a compact, folded particle. We show that Vc defines a ratio, QR, that determines the molecular mass of proteins or RNA ranging from 10 to 1,000 kilodaltons. Furthermore, we propose a statistically robust method for assessing model-data agreements (χ2free) akin to cross-validation. Our approach prevents over-fitting of the SAS data and can be used with a newly defined metric, RSAS, for quantitative evaluation of resolution. Together, these metrics (Vc, QR, χ2free and RSAS) provide analytical tools for unbiased and accurate macromolecular structural characterizations in solution.

Suggested Citation

  • Robert P. Rambo & John A. Tainer, 2013. "Accurate assessment of mass, models and resolution by small-angle scattering," Nature, Nature, vol. 496(7446), pages 477-481, April.
    • Handle: RePEc:nat:nature:v:496:y:2013:i:7446:d:10.1038_nature12070
    DOI: 10.1038/nature12070
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    Cited by:

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