Evidence map›Paper›PMID 33399553›Full record

ArticleJournal of synchrotron radiation2021

High-resolution macromolecular crystallography at the FemtoMAX beamline with time-over-threshold photon detection.

Maja Jensen, Viktor Ahlberg Gagnér, Juan Cabello Sánchez, Åsa U J Bengtsson, J Carl Ekström, Tinna Björg Úlfarsdóttir, Maria Jose Garcia-Bonete, Andrius Jurgilaitis, David Kroon, Van Thai Pham and 9 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of synchrotron radiation, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 90% of its field
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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

19 authors at 4 institutions in 3 countries.

Maja JensenDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.ORCID 0000-0003-4597-8072
Viktor Ahlberg GagnérDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
Juan Cabello SánchezDepartment of Microtechnology and Nanoscience, Chalmers University of Technology, Gothenburg, Sweden.ORCID 0000-0002-9821-3199
Åsa U J BengtssonDepartment of Physics, Lund University, PO Box 118, Lund 22100, Sweden.
J Carl EkströmDepartment of Physics, Lund University, PO Box 118, Lund 22100, Sweden.
Tinna Björg ÚlfarsdóttirDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
Maria Jose Garcia-BoneteDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
Andrius JurgilaitisMAX IV Laboratory, Lund University, PO Box 118, Lund 22100, Sweden.
David KroonMAX IV Laboratory, Lund University, PO Box 118, Lund 22100, Sweden.
Van Thai PhamMAX IV Laboratory, Lund University, PO Box 118, Lund 22100, Sweden.
Stefano ChecciaMAX IV Laboratory, Lund University, PO Box 118, Lund 22100, Sweden.
Hélène Coudert-AlteiracMAX IV Laboratory, Lund University, PO Box 118, Lund 22100, Sweden.
Siawosch SchewaTechnische Hochschule Lübeck, Lübeck, Germany.
Manfred RössleTechnische Hochschule Lübeck, Lübeck, Germany.
Helena RodillaDepartment of Microtechnology and Nanoscience, Chalmers University of Technology, Gothenburg, Sweden.
Jan StakeDepartment of Microtechnology and Nanoscience, Chalmers University of Technology, Gothenburg, Sweden.ORCID 0000-0002-8204-7894
Vitali ZhaunerchykDepartment of Physics, University of Gothenburg, Gothenburg, Sweden.
Jörgen LarssonDepartment of Physics, Lund University, PO Box 118, Lund 22100, Sweden.ORCID 0000-0001-9598-8493
Gergely KatonaDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.ORCID 0000-0002-2031-8716
Lund University · SEUniversity of Gothenburg · SEChalmers University of Technology · SETechnical University of Applied Sciences Lübeck · DE

Funding

Röntgen-Ångström Cluster Framework 2015-06099
6 · The paper itself

Abstract

Protein dynamics contribute to protein function on different time scales. Ultrafast X-ray diffraction snapshots can visualize the location and amplitude of atom displacements after perturbation. Since amplitudes of ultrafast motions are small, high-quality X-ray diffraction data is necessary for detection. Diffraction from bovine trypsin crystals using single femtosecond X-ray pulses was recorded at FemtoMAX, which is a versatile beamline of the MAX IV synchrotron. The time-over-threshold detection made it possible that single photons are distinguishable even under short-pulse low-repetition-rate conditions. The diffraction data quality from FemtoMAX beamline enables atomic resolution investigation of protein structures. This evaluation is based on the shape of the Wilson plot, cumulative intensity distribution compared with theoretical distribution, I/σ, R

Indexed as

Crystallography, X-RayAnimalsCattleMacromolecular SubstancesPhotonsSynchrotronsTrypsinMacromolecular SubstancesTrypsinfemtosecondmacromolecular crystallographymultilayer monochromatortime-over-threshold

Identifiers

PMID33399553
PMCPMC7842217
OpenAlexW3107627436

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.