ArticleJournal of applied crystallography2018
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument.
Article in Journal of applied crystallography, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- The BioSAXS laboratory of the ITACA.SB Research Infrastructure.Journal of applied crystallography · 2026Article
- SAXS Assistant: Automated SAXS analysis for structural discovery in biologics and polymeric nanoparticles.Biophysical journal · 2025Article
- Multi-domain O-GlcNAcase structures reveal allosteric regulatory mechanisms.Nature communications · 2025Article
- Target Engagement Assays in Early Drug Discovery.Journal of medicinal chemistry · 2025Review
- Upgrade of the KWS-2 high-intensity/extended-Journal of applied crystallography · 2025Article
- Size-exclusion chromatography-small-angle neutron scattering system optimized for an instrument with medium neutron flux.Journal of applied crystallography · 2025Article
- Salt-Compact Albumin as a New Pure Protein-based Biomaterials: From Design to In Vivo Studies.Advanced healthcare materials · 2025Article
- Article
- Combined Effects of Pressure and Ionic Strength on Protein-Protein Interactions: An Empirical Approach.Biomacromolecules · 2024Article
- Integrative Approaches to Study Virus Structures.Sub-cellular biochemistry · 2024Review
- Upgraded D22 SEC-SANS setup dedicated to the biology community.Journal of applied crystallography · 2023Article
- Structural insights into redox signal transduction mechanisms in the control of nitrogen fixation by the NifLA system.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Derivation of the small-angle scattering profile of a target biomacromolecule from a profile deteriorated by aggregates. AUC-SAS.Journal of applied crystallography · 2023Article
- Using Small-angle X-ray Scattering to Characterize Biological Systems: A General Overview and Practical Tips.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Hydration in Deep Eutectic Solvents Induces Non-monotonic Changes in the Conformation and Stability of Proteins.Journal of the American Chemical Society · 2022Article
- Inline small-angle X-ray scattering-coupled chromatography under extreme hydrostatic pressure.Protein science : a publication of the Protein Society · 2022Article
- A comparative study of unpasteurized and pasteurized frozen whole hen eggs using size-exclusion chromatography and small-angle X-ray scattering.Scientific reports · 2022Article
- Global fitting of multiple data frames from SEC-SAXS to investigate the structure of next-generation nanodiscs.Acta crystallographica. Section D, Structural biology · 2022Article
- Recent advances in structural characterization of biomacromolecules in foodsFrontiers in nutrition · 2022Review
- Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coupling of size-exclusion chromatography with biological solution small-angle X-ray scattering (SEC-SAXS) on dedicated synchrotron beamlines enables structural analysis of challenging samples such as labile proteins and low-affinity complexes. For this reason, the approach has gained increased popularity during the past decade. Transportation of perishable samples to synchrotrons might, however, compromise the experiments, and the limited availability of synchrotron beamtime renders iterative sample optimization tedious and lengthy. Here, the successful setup of laboratory-based SEC-SAXS is described in a proof-of-concept study. It is demonstrated that sufficient quality data can be obtained on a laboratory instrument with small sample consumption, comparable to typical synchrotron SEC-SAXS demands. UV/vis measurements directly on the SAXS exposure cell ensure accurate concentration determination, crucial for direct molecular weight determination from the scattering data. The absence of radiation damage implies that the sample can be fractionated and subjected to complementary analysis available at the home institution after SEC-SAXS. Laboratory-based SEC-SAXS opens the field for analysis of biological samples at the home institution, thus increasing productivity of biostructural research. It may further ensure that synchrotron beamtime is used primarily for the most suitable and optimized samples.
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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.