Evidence map›Paper›PMID 24914150›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2014

Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers.

Richard Neutze

Abstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. Temporal ghost imaging for pump-probe X-ray solution scattering.Acta crystallographica. Section A, Foundations and advances · 2025
    Article
  3. Article
  4. Deconvolution of dynamic heterogeneity in protein structure.Structural dynamics (Melville, N.Y.) · 2024
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Using photocaging for fast time-resolved structural biology studies.Acta crystallographica. Section D, Structural biology · 2021
    Review
  10. Article
  11. Article
  12. Electron diffraction of CSThe Journal of chemical physics · 2020
    Article
  13. Structural basis of light-harvesting in the photosystem II core complex.Protein science : a publication of the Protein Society · 2020
    Review
  14. Article
  15. Review
  16. Article
  17. Selection of Biophysical Methods for Characterisation of Membrane Proteins.International journal of molecular sciences · 2019
    Review
  18. Strategies for sample delivery for femtosecond crystallography.Acta crystallographica. Section D, Structural biology · 2019
    Review
  19. Article
  20. 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

1 author.

Richard NeutzeDepartment of Chemistry and Molecular Biology, University of Gothenburg, PO Box 462, 40530 Gothenburg, Sweden richard.neutze@chem.gu.se.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

X-ray free-electron lasers (XFELs) are revolutionary X-ray sources. Their time structure, providing X-ray pulses of a few tens of femtoseconds in duration; and their extreme peak brilliance, delivering approximately 10(12) X-ray photons per pulse and facilitating sub-micrometre focusing, distinguish XFEL sources from synchrotron radiation. In this opinion piece, I argue that these properties of XFEL radiation will facilitate new discoveries in life science. I reason that time-resolved serial femtosecond crystallography and time-resolved wide angle X-ray scattering are promising areas of scientific investigation that will be advanced by XFEL capabilities, allowing new scientific questions to be addressed that are not accessible using established methods at storage ring facilities. These questions include visualizing ultrafast protein structural dynamics on the femtosecond to picosecond time-scale, as well as time-resolved diffraction studies of non-cyclic reactions. I argue that these emerging opportunities will stimulate a renaissance of interest in time-resolved structural biochemistry.

Indexed as

ElectronsLasersBiochemistryCrystallography, X-RayProtein ConformationProteinsScattering, RadiationSynchrotronsTime FactorsX-Ray DiffractionProteinsserial femtosecond crystallographystructural biologytime-resolved diffractiontime-resolved wide angle X-ray scatteringX-ray free-electron lasers

Identifiers

PMID24914150
PMCPMC4052859

What OpenQuestion 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 OpenQuestion graph.