Evidence map›Paper›PMID 29739979›Full record

ArticleScientific reports2018

Consensus Bayesian assessment of protein molecular mass from solution X-ray scattering data.

Nelly R Hajizadeh, Daniel Franke, Cy M Jeffries, Dmitri I Svergun

Abstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

115 citing papers in PubMed.

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  8. Disordered N-termini enhance the thermostability of SGNH-hydrolase family polyesterases.Protein science : a publication of the Protein Society · 2026
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  18. Architecture ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  20. Article

55 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Nelly R HajizadehEuropean Molecular Biology Laboratory (EMBL) Hamburg Outstation, DESY, Hamburg, Germany.
Daniel FrankeEuropean Molecular Biology Laboratory (EMBL) Hamburg Outstation, DESY, Hamburg, Germany.
Cy M JeffriesEuropean Molecular Biology Laboratory (EMBL) Hamburg Outstation, DESY, Hamburg, Germany.ORCID 0000-0002-8718-7343
Dmitri I SvergunEuropean Molecular Biology Laboratory (EMBL) Hamburg Outstation, DESY, Hamburg, Germany. svergun@embl-hamburg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molecular mass (MM) is one of the key structural parameters obtained by small-angle X-ray scattering (SAXS) of proteins in solution and is used to assess the sample quality, oligomeric composition and to guide subsequent structural modelling. Concentration-dependent assessment of MM relies on a number of extra quantities (partial specific volume, calibrated intensity, accurate solute concentration) and often yields limited accuracy. Concentration-independent methods forgo these requirements being based on the relationship between structural parameters, scattering invariants and particle volume obtained directly from the data. Using a comparative analysis on 165,982 unique scattering profiles calculated from high-resolution protein structures, the performance of multiple concentration-independent MM determination methods was assessed. A Bayesian inference approach was developed affording an accuracy above that of the individual methods, and reports MM estimates together with a credibility interval. This Bayesian approach can be used in combination with concentration-dependent MM methods to further validate the MM of proteins in solution, or as a reliable stand-alone tool in instances where an accurate concentration estimate is not available.

Indexed as

ConsensusBayes TheoremModels, MolecularMolecular WeightProtein ConformationProteinsScattering, Small AngleSolutionsX-Ray DiffractionProteinsSolutions

Identifiers

PMID29739979
PMCPMC5940760

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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.