Evidence map›Paper›PMID 33731353›Full record

ArticleScience advances2021

Serial femtosecond and serial synchrotron crystallography can yield data of equivalent quality: A systematic comparison.

P Mehrabi, R Bücker, G Bourenkov, H M Ginn, D von Stetten, H M Müller-Werkmeister, A Kuo, T Morizumi, B T Eger, W-L Ou and 15 more

Abstract read
In one paragraph

Article in Science advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
  2. Cefdinir binding to a class A β-lactamase revealed by serial cryo-crystallography.Acta crystallographica. Section D, Structural biology · 2026
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  19. The time revolution in macromolecular crystallography.Structural dynamics (Melville, N.Y.) · 2024
    Article
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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

25 authors.

P MehrabiDepartment for Atomically Resolved Dynamics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany. pedram.mehrabi@mpsd.mpg.de eike.schulz@mpsd.mpg.de.ORCID 0000-0003-3211-6959
R BückerDepartment for Atomically Resolved Dynamics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany.ORCID 0000-0001-7654-4707
G BourenkovEuropean Molecular Biology Laboratory (EMBL), Hamburg Outstation c/o Deutsches Elektronen-Synchrotron (DESY), Notkestraße 85, D-22603 Hamburg, Germany.ORCID 0000-0002-2617-5920
H M GinnDiamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, UK.
D von StettenEuropean Molecular Biology Laboratory (EMBL), Hamburg Outstation c/o Deutsches Elektronen-Synchrotron (DESY), Notkestraße 85, D-22603 Hamburg, Germany.ORCID 0000-0001-7906-9788
H M Müller-WerkmeisterInstitute of Chemistry-Physical Chemistry, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam-Golm, Germany.ORCID 0000-0001-9471-882X
A KuoDepartment of Biochemistry, University of Toronto, 1 King's College Circle, Toronto, Ontario M5S 1A8, Canada.ORCID 0000-0002-4234-6320
T MorizumiDepartment of Biochemistry, University of Toronto, 1 King's College Circle, Toronto, Ontario M5S 1A8, Canada.ORCID 0000-0002-2785-209X
B T EgerDepartment of Biochemistry, University of Toronto, 1 King's College Circle, Toronto, Ontario M5S 1A8, Canada.ORCID 0000-0003-3350-9332
W-L OuDepartment of Biochemistry, University of Toronto, 1 King's College Circle, Toronto, Ontario M5S 1A8, Canada.ORCID 0000-0002-8069-5927
S OghbaeyDepartments of Chemistry and Physics, University of Toronto, 80 St. George Street, Toronto, Ontario M5S 3H6, Canada.ORCID 0000-0003-3580-655X
A SarraciniDepartments of Chemistry and Physics, University of Toronto, 80 St. George Street, Toronto, Ontario M5S 3H6, Canada.
J E BesawDepartment of Biochemistry, University of Toronto, 1 King's College Circle, Toronto, Ontario M5S 1A8, Canada.ORCID 0000-0002-7571-7132
O Pare-LabrosseDepartment for Atomically Resolved Dynamics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany.ORCID 0000-0001-9241-8356
S MeierDepartment of Physics, Universität Hamburg, Jungiusstrasse 9, 20355 Hamburg, Germany.
H SchikoraScientific Support Unit Machine Physics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany.ORCID 0000-0002-4778-6982
F TellkampScientific Support Unit Machine Physics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany.ORCID 0000-0002-5670-3544
A MarxDepartment for Atomically Resolved Dynamics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany.
D A SherrellDiamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, UK.ORCID 0000-0002-6393-8800
D AxfordDiamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, UK.ORCID 0000-0001-7694-8525
R L OwenDiamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, UK.ORCID 0000-0002-2104-7057
O P ErnstDepartment of Biochemistry, University of Toronto, 1 King's College Circle, Toronto, Ontario M5S 1A8, Canada.ORCID 0000-0002-8863-9444
E F PaiDepartment of Medical Biophysics, University of Toronto, 101 College Street, Toronto, Ontario M5G 1L7, Canada.ORCID 0000-0002-1162-7242
E C SchulzDepartment for Atomically Resolved Dynamics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany. pedram.mehrabi@mpsd.mpg.de eike.schulz@mpsd.mpg.de.ORCID 0000-0002-1685-8605
R J D MillerDepartment for Atomically Resolved Dynamics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany.ORCID 0000-0003-0884-0541

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For the two proteins myoglobin and fluoroacetate dehalogenase, we present a systematic comparison of crystallographic diffraction data collected by serial femtosecond (SFX) and serial synchrotron crystallography (SSX). To maximize comparability, we used the same batch of micron-sized crystals, the same sample delivery device, and the same data analysis software. Overall figures of merit indicate that the data of both radiation sources are of equivalent quality. For both proteins, reasonable data statistics can be obtained with approximately 5000 room-temperature diffraction images irrespective of the radiation source. The direct comparability of SSX and SFX data indicates that the quality of diffraction data obtained from these samples is linked to the properties of the crystals rather than to the radiation source. Therefore, for other systems with similar properties, time-resolved experiments can be conducted at the radiation source that best matches the desired time resolution.

Indexed as

ProteinsSynchrotronsCrystallography, X-RayProteins

Identifiers

PMID33731353
PMCPMC7968842

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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.