Evidence map›Paper›PMID 36048152›Full record

ArticleActa crystallographica. Section D, Structural biology2022

Medical contrast agents as promising tools for biomacromolecular SAXS experiments.

Frank Gabel, Sylvain Engilberge, Emmanuelle Schmitt, Aurélien Thureau, Yves Mechulam, Javier Pérez, Eric Girard

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

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.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Structural characterization of humanFrontiers in oncology · 2023
    Article
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

7 authors.

Frank GabelIBS, CEA, CNRS, UGA, 71 Avenue des Martyrs, 38000 Grenoble, France.ORCID 0000-0003-3446-2601
Sylvain EngilbergeIBS, CEA, CNRS, UGA, 71 Avenue des Martyrs, 38000 Grenoble, France.ORCID 0000-0001-8680-6790
Emmanuelle SchmittIOC, Ecole polytechnique, CNRS, Institut Polytechnique de Paris, 91128 Palaiseau, France.
Aurélien ThureauSynchrotron SOLEIL, Saint-Aubin BP 48, 91192 Gif-sur-Yvette, France.
Yves MechulamIOC, Ecole polytechnique, CNRS, Institut Polytechnique de Paris, 91128 Palaiseau, France.
Javier PérezSynchrotron SOLEIL, Saint-Aubin BP 48, 91192 Gif-sur-Yvette, France.
Eric GirardIBS, CEA, CNRS, UGA, 71 Avenue des Martyrs, 38000 Grenoble, France.ORCID 0000-0002-5758-6095

Funding

Agence Nationale de la Recherche ANR-13-BS07-0007Agence Nationale de la Recherche ANR-21-CE11-0025
6 · The paper itself

Abstract

Small-angle X-ray scattering (SAXS) has become an indispensable tool in structural biology, complementing atomic-resolution techniques. It is sensitive to the electron-density difference between solubilized biomacromolecules and the buffer, and provides information on molecular masses, particle dimensions and interactions, low-resolution conformations and pair distance-distribution functions. When SAXS data are recorded at multiple contrasts, i.e. at different solvent electron densities, it is possible to probe, in addition to their overall shape, the internal electron-density profile of biomacromolecular assemblies. Unfortunately, contrast-variation SAXS has been limited by the range of solvent electron densities attainable using conventional co-solutes (for example sugars, glycerol and salt) and by the fact that some biological systems are destabilized in their presence. Here, SAXS contrast data from an oligomeric protein and a protein-RNA complex are presented in the presence of iohexol and Gd-HPDO3A, two electron-rich molecules that are used in biomedical imaging and that belong to the families of iodinated and lanthanide-based complexes, respectively. Moderate concentrations of both molecules allowed solvent electron densities matching those of proteins to be attained. While iohexol yielded higher solvent electron densities (per mole), it interacted specifically with the oligomeric protein and precipitated the protein-RNA complex. Gd-HPDO3A, while less efficient (per mole), did not disrupt the structural integrity of either system, and atomic models could be compared with the SAXS data. Due to their elevated solubility and electron density, their chemical inertness, as well as the possibility of altering their physico-chemical properties, lanthanide-based complexes represent a class of molecules with promising potential for contrast-variation SAXS experiments on diverse biomacromolecular systems.

Indexed as

Contrast MediaLanthanoid Series ElementsIohexolProteinsRNAScattering, Small AngleSolventsX-Ray DiffractionContrast MediaIohexolLanthanoid Series ElementsProteinsRNASolventscontrast variationelectron densityGd-HPDO3Aiohexolmacromolecular complexesmedical contrast agentsSAXSsmall-angle scatteringtools for SAXS

Identifiers

PMID36048152
PMCPMC9435597

What Socratic holds

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LicenceCC BY
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Registered trials

None linked

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 Socratic graph.