Cited by 750Enzyme Structure and FunctionProtein Structure and DynamicsNuclear Physics and Applications

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

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Rambo, Robert P., Tainer, John A.·2013·Nature

DOI 10.1038/nature12070PMC PMC3714217

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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 (χ(2)free) 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, χ(2)free and RSAS) provide analytical tools for unbiased and accurate macromolecular structural characterizations in solution.

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Self-citation
TRYBE®: an Fc-free antibody format with three monovalent targeting arms engineered for long in vivo half-life
Davé, E., Durrant, O., Dhami, N., Compson, J. E., Broadbridge, J., Archer, S., Maroof, A., Whale, K., Ménochet, K., Bonnaillie, P., et al. (2023) · mAbs · doi:10.1080/19420862.2022.2160229 · Cited by 3

Authors: Rambo, R. P., & Tainer, J. A.
Affiliations: Lawrence Berkeley National Laboratory (US)
Scripps Research Institute (US)
Corresponding author: Rambo, Robert P.
Tainer, John A.
ORCID: Rambo, Robert P.
Tainer, John A.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2013-04
Volume: 496
Issue: 7446
Pages: 477-481
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature12070
PMC: PMC3714217
OpenAlex: W1984084102
Cited by: 750
References: 35
Citations by year: 2026: 34 · 2025: 34 · 2024: 39 · 2023: 46 · 2022: 81 · 2021: 57 · 2020: 71 · 2019: 65 · 2018: 64 · 2017: 70 · 2016: 74 · 2015: 53 · 2014: 43 · 2013: 19
FWCI: 28.41
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Funders: National Cancer Institute (R35CA220430)
National Institute of General Medical Sciences (R01GM105404)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Physics and Astronomy › Radiation › Nuclear Physics and Applications
Keywords: small-angle scattering, molecular mass estimation, model-data agreement, resolution assessment, model validation, protein complexes, macromolecular flexibility, solution structure
MeSH terms: DNA-Binding Proteins, Models, Chemical, Models, Molecular, Molecular Conformation, Molecular Weight, RNA, Viral, Solutions, Reproducibility of Results, RNA-Binding Proteins, Pliability, Aldose-Ketose Isomerases, Scattering, Small Angle, Riboswitch

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