Evidence map›Paper›PMID 39572886›Full record

ArticleFEBS open bio2025

Protein crystallization and structure determination at room temperature in the CrystalChip.

Petr Pachl, Léna Coudray, Romain Vincent, Léa Nilles, Hélène Scheer, Christophe Ritzenthaler, Adéla Fejfarová, Pavlína Řezáčová, Sylvain Engilberge, Claude Sauter

Abstract read
In one paragraph

Article in FEBS open bio, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
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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

10 authors.

Petr PachlCNRS, Architecture et Réactivité de l'ARN, UPR 9002, Institut de Biologie Moléculaire et Cellulaire, Université de Strasbourg, France.ORCID https://orcid.org/0000-0001-9215-9817
Léna CoudrayCNRS, Architecture et Réactivité de l'ARN, UPR 9002, Institut de Biologie Moléculaire et Cellulaire, Université de Strasbourg, France.
Romain VincentCNRS, Architecture et Réactivité de l'ARN, UPR 9002, Institut de Biologie Moléculaire et Cellulaire, Université de Strasbourg, France.ORCID https://orcid.org/0009-0004-0542-3384
Léa NillesCNRS, Architecture et Réactivité de l'ARN, UPR 9002, Institut de Biologie Moléculaire et Cellulaire, Université de Strasbourg, France.
Hélène ScheerCNRS, Institut de Biologie Moléculaire des plantes, UPR 2357, Université de Strasbourg, France.
Christophe RitzenthalerCNRS, Institut de Biologie Moléculaire des plantes, UPR 2357, Université de Strasbourg, France.
Adéla FejfarováInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Praha 6, Czech Republic.ORCID https://orcid.org/0009-0002-8953-4377
Pavlína ŘezáčováInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Praha 6, Czech Republic.
Sylvain EngilbergeCNRS, CEA, Institut de Biologie Structurale (IBS), Université Grenoble Alpes, France.
Claude SauterCNRS, Architecture et Réactivité de l'ARN, UPR 9002, Institut de Biologie Moléculaire et Cellulaire, Université de Strasbourg, France.ORCID https://orcid.org/0000-0002-8766-287X

Funding

Czech Ministry for Education, Youth and Sports 8J23FR035French Centre National de la Recherche Scientifique (CNRS)French Ministry for Europe and Foreign AffairsFrench Ministry for Higher Education and Research 49306SCInstitut des Sciences Biologiques (10.13039/501100017210 - CNRS biologie)Laboratoire d'Excellence NetRNA ANR-10-LABX-0036_NETRNANextGenerationEU LX22NPO5102Université de Strasbourg USIAS-W21RSAUT
6 · The paper itself

Abstract

The production of high-quality crystals is a key step in crystallography in general, but control of crystallization conditions is even more crucial in serial crystallography, which requires sets of crystals homogeneous in size and diffraction properties. This protocol describes the implementation of a simple and user-friendly microfluidic device that allows both the production of crystals by the counter-diffusion method and their in situ analysis by serial crystallography. As an illustration, the whole procedure is used to determine the crystal structure of three proteins from data collected at room temperature at a synchrotron radiation source.

Indexed as

ProteinsCrystallizationCrystallography, X-RayProtein ConformationTemperatureProteinsCrystalChipcrystallizationmicrocrystalsmicrofluidicsserial crystallography

Identifiers

PMID39572886
PMCPMC11961392

What OpenQuestion holds

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Registered trials

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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.