ArticleIUCrJ2015
A posteriori determination of the useful data range for small-angle scattering experiments on dilute monodisperse systems.
Article in IUCrJ, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- SAStutorials.org - online tutorials on small-angle scattering data analysis.Journal of applied crystallography · 2025Article
- Dimerization of ADAR1 modulates site-specificity of RNA editing.Nature communications · 2024Article
- The disordered C-terminal tail of fungal LPMOs from phytopathogens mediates protein dimerization and impacts plant penetration.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- RNA 3D structure modeling by fragment assembly with small-angle X-ray scattering restraints.Bioinformatics (Oxford, England) · 2023Article
- The structure ofFrontiers in immunology · 2023Article
- Visualizing and accessing correlated SAXS data sets with Similarity Maps and Simple Scattering web resources.Methods in enzymology · 2023Article
- Describing small-angle scattering profiles by a limited set of intensities.Journal of applied crystallography · 2022Article
- SAXSMoW 3.0: New advances in the determination of the molecular weight of proteins in dilute solutions from SAXS intensity data on a relative scale.Protein science : a publication of the Protein Society · 2022Article
- EFAMIX, a tool to decompose inline chromatography SAXS data from partially overlapping components.Protein science : a publication of the Protein Society · 2022Article
- Refining conformational ensembles of flexible proteins against small-angle x-ray scattering data.Biophysical journal · 2021Article
- Periscope Proteins are variable-length regulators of bacterial cell surface interactions.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural basis for DNA recognition and allosteric control of the retinoic acid receptors RAR-RXR.Nucleic acids research · 2020Article
- Structural analysis of the LDL receptor-interacting FERM domain in the E3 ubiquitin ligase IDOL reveals an obscured substrate-binding site.The Journal of biological chemistry · 2020Article
- Structure of a collagen VI α3 chain VWA domain array: adaptability and functional implications of myopathy causing mutations.The Journal of biological chemistry · 2020Article
- Low-resolution molecular shape, biochemical characterization and emulsification properties of a halotolerant esterase from Bacillus licheniformis.European biophysics journal : EBJ · 2020Article
- RovC - a novel type of hexameric transcriptional activator promoting type VI secretion gene expression.PLoS pathogens · 2020Article
- Combining molecular dynamics simulations with small-angle X-ray and neutron scattering data to study multi-domain proteins in solution.PLoS computational biology · 2020Article
- SASBDB: Towards an automatically curated and validated repository for biological scattering data.Protein science : a publication of the Protein Society · 2020Article
- Methods, development and applications of small-angle X-ray scattering to characterize biological macromolecules in solution.Current research in structural biology · 2020Review
- Extended Experimental Inferential Structure Determination Method in Determining the Structural Ensembles of Disordered Protein States.Communications chemistry · 2020Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small-angle X-ray and neutron scattering (SAXS and SANS) experiments on solutions provide rapidly decaying scattering curves, often with a poor signal-to-noise ratio, especially at higher angles. On modern instruments, the noise is partially compensated for by oversampling, thanks to the fact that the angular increment in the data is small compared with that needed to describe adequately the local behaviour and features of the scattering curve. Given a (noisy) experimental data set, an important question arises as to which part of the data still contains useful information and should be taken into account for the interpretation and model building. Here, it is demonstrated that, for monodisperse systems, the useful experimental data range is defined by the number of meaningful Shannon channels that can be determined from the data set. An algorithm to determine this number and thus the data range is developed, and it is tested on a number of simulated data sets with various noise levels and with different degrees of oversampling, corresponding to typical SAXS/SANS experiments. The method is implemented in a computer program and examples of its application to analyse the experimental data recorded under various conditions are presented. The program can be employed to discard experimental data containing no useful information in automated pipelines, in modelling procedures, and for data deposition or publication. The software is freely accessible to academic users.
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