Evidence map›Paper›PMID 27158504›Full record

ArticleIUCrJ2016

Protein structure determination by single-wavelength anomalous diffraction phasing of X-ray free-electron laser data.

Karol Nass, Anton Meinhart, Thomas R M Barends, Lutz Foucar, Alexander Gorel, Andrew Aquila, Sabine Botha, R Bruce Doak, Jason Koglin, Mengning Liang and 4 more

Abstract read
In one paragraph

Article in IUCrJ, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. XFEL Microcrystallography of Self-Assembling SilverJournal of the American Chemical Society · 2023
    Article
  7. Review
  8. Article
  9. Serial femtosecond crystallography.Nature reviews. Methods primers · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. High-throughput in situ experimental phasing.Acta crystallographica. Section D, Structural biology · 2020
    Article
  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

14 authors.

Karol NassDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research , Jahnstrasse 29, 69120 Heidelberg, Germany.
Anton MeinhartDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research , Jahnstrasse 29, 69120 Heidelberg, Germany.
Thomas R M BarendsDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research , Jahnstrasse 29, 69120 Heidelberg, Germany.
Lutz FoucarDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research , Jahnstrasse 29, 69120 Heidelberg, Germany.
Alexander GorelDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research , Jahnstrasse 29, 69120 Heidelberg, Germany.
Andrew AquilaEuropean XFEL GmbH , Albert-Einstein-Ring 19, 22761 Hamburg, Germany.
Sabine BothaDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research , Jahnstrasse 29, 69120 Heidelberg, Germany.
R Bruce DoakDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research , Jahnstrasse 29, 69120 Heidelberg, Germany.
Jason KoglinSLAC National Accelerator Laboratory , 2575 Sand Hill Road, Menlo Park, CA 94025, USA.
Mengning LiangSLAC National Accelerator Laboratory , 2575 Sand Hill Road, Menlo Park, CA 94025, USA.
Robert L ShoemanDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research , Jahnstrasse 29, 69120 Heidelberg, Germany.
Garth WilliamsSLAC National Accelerator Laboratory , 2575 Sand Hill Road, Menlo Park, CA 94025, USA.
Sebastien BoutetSLAC National Accelerator Laboratory , 2575 Sand Hill Road, Menlo Park, CA 94025, USA.
Ilme SchlichtingDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research , Jahnstrasse 29, 69120 Heidelberg, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) offers unprecedented possibilities for macromolecular structure determination of systems that are prone to radiation damage. However, phasing XFEL data de novo is complicated by the inherent inaccuracy of SFX data, and only a few successful examples, mostly based on exceedingly strong anomalous or isomorphous difference signals, have been reported. Here, it is shown that SFX data from thaumatin microcrystals can be successfully phased using only the weak anomalous scattering from the endogenous S atoms. Moreover, a step-by-step investigation is presented of the particular problems of SAD phasing of SFX data, analysing data from a derivative with a strong anomalous signal as well as the weak signal from endogenous S atoms.

Indexed as

SAD phasingserial femtosecond crystallographySFXsingle-wavelength anomalous diffractionXFELsX-ray free-electron lasers

Identifiers

PMID27158504
PMCPMC4856140

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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.