ArticleJournal of applied crystallography2017
Quantitative evaluation of statistical errors in small-angle X-ray scattering measurements.
Article in Journal of applied crystallography, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Assessing protein-specific radiation damage in time-resolved X-ray solution-scattering experiments at high-brilliance synchrotrons using fast detector readout.Acta crystallographica. Section D, Structural biology · 2026Article
- Optimal weights and priors in simultaneous fitting of multiple small-angle scattering datasets.Journal of applied crystallography · 2025Article
- Retrieving the size distribution of SBA-15 mesopores from small-angle X-ray scattering data using a Monte Carlo method.Journal of applied crystallography · 2023Article
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- Contrast variation SAXS: Sample preparation protocols, experimental procedures, and data analysis.Methods in enzymology · 2022Article
- Small angle X-ray scattering analysis of ligand-bound forms of tetrameric apolipoprotein-D.Bioscience reports · 2021Article
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- Estimating signal and noise of time-resolved X-ray solution scattering data at synchrotrons and XFELs.Journal of synchrotron radiation · 2020Article
- Extended Experimental Inferential Structure Determination Method in Determining the Structural Ensembles of Disordered Protein States.Communications chemistry · 2020Article
- The role of small-angle scattering in structure-based screening applications.Biophysical reviews · 2018Review
- Predicting data quality in biological X-ray solution scattering.Acta crystallographica. Section D, Structural biology · 2018Review
- 2017 publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution: an update.Acta crystallographica. Section D, Structural biology · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new model is proposed for the measurement errors incurred in typical small-angle X-ray scattering (SAXS) experiments, which takes into account the setup geometry and physics of the measurement process. The model accurately captures the experimentally determined errors from a large range of synchrotron and in-house anode-based measurements. Its most general formulation gives for the variance of the buffer-subtracted SAXS intensity σ
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.