Evidence map›Paper›PMID 24914146›Full record

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

Diffraction before destruction.

Henry N Chapman, Carl Caleman, Nicusor Timneanu

Abstract read
In one paragraph

Article 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 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing 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

112 citing papers in PubMed.

  1. Article
  2. Radiation damage in serial femtosecond crystallography studied in hemoglobin.Acta crystallographica. Section D, Structural biology · 2026
    Article
  3. Article
  4. Automated serial electron diffraction: implementation inJournal of applied crystallography · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. A Bright and Dynamic Future in Structural Biology.Advances in experimental medicine and biology · 2026
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

52 more citing papers are in PubMed but not listed here.

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

3 authors.

Henry N ChapmanCenter for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany Department of Physics, University of Hamburg, Luruper Chaussee 149, 22761 Hamburg, Germany Centre for Ultrafast Imaging, Luruper Chaussee 149, 22761 Hamburg, Germany henry.chapman@desy.de.
Carl CalemanCenter for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany Department of Physics and Astronomy, Uppsala University, Box 516, 75120 Uppsala, Sweden.
Nicusor TimneanuDepartment of Physics and Astronomy, Uppsala University, Box 516, 75120 Uppsala, Sweden Laboratory of Molecular Biophysics, Department of Cell and Molecular Biology, Uppsala University, Box 596, 75124 Uppsala, Sweden.

Funding

Wellcome Trust 102593
6 · The paper itself

Abstract

X-ray free-electron lasers have opened up the possibility of structure determination of protein crystals at room temperature, free of radiation damage. The femtosecond-duration pulses of these sources enable diffraction signals to be collected from samples at doses of 1000 MGy or higher. The sample is vaporized by the intense pulse, but not before the scattering that gives rise to the diffraction pattern takes place. Consequently, only a single flash diffraction pattern can be recorded from a crystal, giving rise to the method of serial crystallography where tens of thousands of patterns are collected from individual crystals that flow across the beam and the patterns are indexed and aggregated into a set of structure factors. The high-dose tolerance and the many-crystal averaging approach allow data to be collected from much smaller crystals than have been examined at synchrotron radiation facilities, even from radiation-sensitive samples. Here, we review the interaction of intense femtosecond X-ray pulses with materials and discuss the implications for structure determination. We identify various dose regimes and conclude that the strongest achievable signals for a given sample are attained at the highest possible dose rates, from highest possible pulse intensities.

Indexed as

ElectronsLasersProtein ConformationProteinsX-Ray DiffractionProteinsprotein crystallographyradiation damageX-ray lasers

Identifiers

PMID24914146
PMCPMC4052855

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.