ReviewIUCrJ2017
Progress in small-angle scattering from biological solutions at high-brilliance synchrotrons.
Review in IUCrJ, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed.
- The BioSAXS laboratory of the ITACA.SB Research Infrastructure.Journal of applied crystallography · 2026Article
- Small Angle Scattering Techniques on In Situ Adsorption Studies: A Comprehensive Review.Materials (Basel, Switzerland) · 2026Review
- Integrated analysis with iCM-SANS, SAXS and MD simulations for dynamics of multi-domain proteins.Journal of applied crystallography · 2026Article
- Selective deuteration of an RNA:RNA complex for structural analysis using small-angle scattering.Structure (London, England : 1993) · 2025Article
- Selective deuteration of an RNA:RNA complex for structural analysis using small-angle scattering.bioRxiv : the preprint server for biology · 2024Article
- Accurate and Efficient SAXS/SANS Implementation Including Solvation Layer Effects Suitable for Molecular Simulations.Journal of chemical theory and computation · 2023Article
- Persistence Length of PEGMA Bottle Brushes Determined by Pyrene Excimer Fluorescence.Polymers · 2023Article
- Enabling Efficient Design of Biological Formulations Through Advanced Characterization.Pharmaceutical research · 2023Review
- Structural studies of protein-nucleic acid complexes: A brief overview of the selected techniques.Computational and structural biotechnology journal · 2023Review
- The solution structure of the unbound IgG Fc receptor CD64 resembles its crystal structure: Implications for function.PloS one · 2023Article
- A round-robin approach provides a detailed assessment of biomolecular small-angle scattering data reproducibility and yields consensus curves for benchmarking.Acta crystallographica. Section D, Structural biology · 2022Article
- Medical contrast agents as promising tools for biomacromolecular SAXS experiments.Acta crystallographica. Section D, Structural biology · 2022Article
- Cluster Size of Amylopectin and Nanosized Amylopectin Fragments Characterized by Pyrene Excimer Formation.Polymers · 2022Article
- Cross-validation of distance measurements in proteins by PELDOR/DEER and single-molecule FRET.Nature communications · 2022Article
- Article
- Small-angle scattering for beginners.Journal of applied crystallography · 2021Article
- Integrated sample-handling and mounting system for fixed-target serial synchrotron crystallography.Acta crystallographica. Section D, Structural biology · 2021Article
- Article
- Physics of viral dynamics.Nature reviews. Physics · 2021Review
- Quantitative comparison between sub-millisecond time resolution single-molecule FRET measurements and 10-second molecular simulations of a biosensor protein.PLoS computational biology · 2020Article
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small-angle X-ray scattering (SAXS) is an established technique that provides low-resolution structural information on macromolecular solutions. Recent decades have witnessed significant progress in both experimental facilities and in novel data-analysis approaches, making SAXS a mainstream method for structural biology. The technique is routinely applied to directly reconstruct low-resolution shapes of proteins and to generate atomistic models of macromolecular assemblies using hybrid approaches. Very importantly, SAXS is capable of yielding structural information on systems with size and conformational polydispersity, including highly flexible objects. In addition, utilizing high-flux synchrotron facilities, time-resolved SAXS allows analysis of kinetic processes over time ranges from microseconds to hours. Dedicated bioSAXS beamlines now offer fully automated data-collection and analysis pipelines, where analysis and modelling is conducted on the fly. This enables SAXS to be employed as a high-throughput method to rapidly screen various sample conditions and additives. The growing SAXS user community is supported by developments in data and model archiving and quality criteria. This review illustrates the latest developments in SAXS, in particular highlighting time-resolved applications aimed at flexible and evolving systems.
Indexed as
Identifiers
What OpenQuestion holds
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.