Evidence map›Paper›PMID 36381146›Full record

ArticleIUCrJ2022

Slow protein dynamics probed by time-resolved oscillation crystallography at room temperature.

Sylvain Aumonier, Sylvain Engilberge, Nicolas Caramello, David von Stetten, Guillaume Gotthard, Gordon A Leonard, Christoph Mueller-Dieckmann, Antoine Royant

Abstract read
In one paragraph

Article in IUCrJ, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. TheJournal of applied crystallography · 2025
    Article
  4. Article
  5. The time revolution in macromolecular crystallography.Structural dynamics (Melville, N.Y.) · 2024
    Article
  6. Article
  7. Review
  8. Article
  9. Introduction to the virtual thematic issue on room-temperature biological crystallography.Acta crystallographica. Section F, Structural biology communications · 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

8 authors.

Sylvain AumonierStructural Biology Group, European Synchrotron Radiation Facility, 71 avenue des Martyrs CS 40220, Grenoble 38043, France.ORCID https://orcid.org/0000-0002-1568-2150
Sylvain EngilbergeStructural Biology Group, European Synchrotron Radiation Facility, 71 avenue des Martyrs CS 40220, Grenoble 38043, France.ORCID https://orcid.org/0000-0001-8680-6790
Nicolas CaramelloStructural Biology Group, European Synchrotron Radiation Facility, 71 avenue des Martyrs CS 40220, Grenoble 38043, France.ORCID https://orcid.org/0000-0003-0025-0213
David von StettenStructural Biology Group, European Synchrotron Radiation Facility, 71 avenue des Martyrs CS 40220, Grenoble 38043, France.ORCID https://orcid.org/0000-0001-7906-9788
Guillaume GotthardStructural Biology Group, European Synchrotron Radiation Facility, 71 avenue des Martyrs CS 40220, Grenoble 38043, France.ORCID https://orcid.org/0000-0003-2830-0286
Gordon A LeonardStructural Biology Group, European Synchrotron Radiation Facility, 71 avenue des Martyrs CS 40220, Grenoble 38043, France.ORCID https://orcid.org/0000-0001-5030-0122
Christoph Mueller-DieckmannStructural Biology Group, European Synchrotron Radiation Facility, 71 avenue des Martyrs CS 40220, Grenoble 38043, France.ORCID https://orcid.org/0000-0003-3625-2747
Antoine RoyantUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), 71 avenue des Martyrs, Grenoble 38044, France.ORCID https://orcid.org/0000-0002-1919-8649

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The development of serial crystallography over the last decade at XFELs and synchrotrons has produced a renaissance in room-temperature macromolecular crystallography (RT-MX), and fostered many technical and methodological breakthroughs designed to study phenomena occurring in proteins on the picosecond-to-second timescale. However, there are components of protein dynamics that occur in much slower regimes, of which the study could readily benefit from state-of-the-art RT-MX. Here, the room-temperature structural study of the relaxation of a reaction intermediate at a synchrotron, exploiting a handful of single crystals, is described. The intermediate in question is formed in microseconds during the photoreaction of the LOV2 domain of phototropin 2 from

Indexed as

LOV2 domain of phototropin 2protein dynamicsroom-temperature crystallographytime-resolved crystallography

Identifiers

PMID36381146
PMCPMC9634615

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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.