Evidence map›Paper›PMID 28009549›Full record

ArticleJournal of synchrotron radiation2017

Bragg coherent diffraction imaging and metrics for radiation damage in protein micro-crystallography.

H D Coughlan, C Darmanin, H J Kirkwood, N W Phillips, D Hoxley, J N Clark, D J Vine, F Hofmann, R J Harder, E Maxey and 1 more

Abstract read
In one paragraph

Article in Journal of synchrotron radiation, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Damage-limited resolution for X-ray and electron microscopy of organic specimens.Acta crystallographica. Section D, Structural biology · 2026
    Article
  2. How Beam Damage Can Skew SynchrotronACS energy letters · 2023
    Article
  3. Article
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  9. Simulated sample heating from a nanofocused X-ray beam.Journal of synchrotron radiation · 2017
    Article
  10. 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

11 authors.

H D CoughlanARC Centre of Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University, Victoria 3086, Australia.
C DarmaninARC Centre of Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University, Victoria 3086, Australia.
H J KirkwoodARC Centre of Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University, Victoria 3086, Australia.
N W PhillipsARC Centre of Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University, Victoria 3086, Australia.
D HoxleyARC Centre of Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University, Victoria 3086, Australia.
J N ClarkStanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
D J VineAdvanced Light Source, Berkeley Lab, Berkeley, CA 94720, USA.
F HofmannDepartment of Engineering Science, University of Oxford, Oxford OX1 3PJ, UK.
R J HarderAdvanced Photon Source, Argonne National Laboratory, Argonne, IL 60439, USA.
E MaxeyAdvanced Photon Source, Argonne National Laboratory, Argonne, IL 60439, USA.
B AbbeyARC Centre of Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University, Victoria 3086, Australia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proliferation of extremely intense synchrotron sources has enabled ever higher-resolution structures to be obtained using data collected from smaller and often more imperfect biological crystals (Helliwell, 1984). Synchrotron beamlines now exist that are capable of measuring data from single crystals that are just a few micrometres in size. This provides renewed motivation to study and understand the radiation damage behaviour of small protein crystals. Reciprocal-space mapping and Bragg coherent diffractive imaging experiments have been performed on cryo-cooled microcrystals of hen egg-white lysozyme as they undergo radiation damage. Several well established metrics, such as intensity-loss and lattice expansion, are applied to the diffraction data and the results are compared with several new metrics that can be extracted from the coherent imaging experiments. Individually some of these metrics are inconclusive. However, combining metrics, the results suggest that radiation damage behaviour in protein micro-crystals differs from that of larger protein crystals and may allow them to continue to diffract for longer. A possible mechanism to account for these observations is proposed.

Indexed as

Crystallography, X-RaySynchrotronsAnimalsChickensFemaleProteinsProteinsBragg coherent diffractive imagingdosemicro-crystallographyprotein crystallographyradiation damage

Identifiers

PMID28009549
PMCPMC5182022

What OpenQuestion holds

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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.