Evidence map›Paper›PMID 28574461›Full record

ArticleSensors (Basel, Switzerland)2017

Innovative High-Throughput SAXS Methodologies Based on Photonic Lab-on-a-Chip Sensors: Application to Macromolecular Studies.

Isaac Rodríguez-Ruiz, Dimitri Radajewski, Sophie Charton, Nhat Phamvan, Martha Brennich, Petra Pernot, Françoise Bonneté, Sébastien Teychené

Abstract read
In one paragraph

Article in Sensors (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Microfluidic devices for small-angle neutron scattering.Journal of applied crystallography · 2018
    Review
  8. Review
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

8 authors.

Isaac Rodríguez-RuizCEA, DEN, DMRC, SA2I, 30207 Bagnols-sur-Cèze, France. isaac.rodriguez-ruiz@cea.fr.
Dimitri RadajewskiLaboratoire de Génie Chimique, UMR 5503, 4 allée Emile Monso, 31432 Toulouse, France. dimitri.radajewski@ensiacet.fr.
Sophie ChartonCEA, DEN, DMRC, SA2I, 30207 Bagnols-sur-Cèze, France. sophie.charton@cea.fr.
Nhat PhamvanLaboratoire de Génie Chimique, UMR 5503, 4 allée Emile Monso, 31432 Toulouse, France. nhatpv.coltech@gmail.com.
Martha BrennichEuropean Molecular Biology Laboratory, 71 avenue des Martyrs, 38000 Grenoble, France. martha.brennich@esrf.fr.
Petra PernotEuropean Molecular Biology Laboratory, 71 avenue des Martyrs, 38000 Grenoble, France. rejma@esrf.fr.
Françoise BonnetéInstitut des Biomolécules Max-Mousseron, UMR 5247, Université d'Avignon, 33 rue Louis Pasteur, 84000 Avignon, France. francoise.bonnete@univ-avignon.fr.
Sébastien TeychenéLaboratoire de Génie Chimique, UMR 5503, 4 allée Emile Monso, 31432 Toulouse, France. sebastien.teychene@ensiacet.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The relevance of coupling droplet-based Photonic Lab-on-a-Chip (PhLoC) platforms and Small-Angle X-Ray Scattering (SAXS) technique is here highlighted for the performance of high throughput investigations, related to the study of protein macromolecular interactions. With this configuration, minute amounts of sample are required to obtain reliable statistical data. The PhLoC platforms presented in this work are designed to allow and control an effective mixing of precise amounts of proteins, crystallization reagents and buffer in nanoliter volumes, and the subsequent generation of nanodroplets by means of a two-phase flow. Spectrophotometric sensing permits a fine control on droplet generation frequency and stability as well as on concentration conditions, and finally the droplet flow is synchronized to perform synchrotron radiation SAXS measurements in individual droplets (each one acting as an isolated microreactor) to probe protein interactions. With this configuration, droplet physic-chemical conditions can be reproducibly and finely tuned, and monitored without cross-contamination, allowing for the screening of a substantial number of saturation conditions with a small amount of biological material. The setup was tested and validated using lysozyme as a model of study. By means of SAXS experiments, the proteins gyration radius and structure envelope were calculated as a function of protein concentration. The obtained values were found to be in good agreement with previously reported data, but with a dramatic reduction of sample volume requirements compared to studies reported in the literature.

Indexed as

microfluidicsPhotonic Lab-on-a-Chipprotein interactionsSAXSspectrophotometric detection

Identifiers

PMID28574461
PMCPMC5492703

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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 OpenQuestion graph.