Evidence map›Paper›PMID 29354276›Full record

ArticleIUCrJ2018

Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals.

Cecilia M Casadei, Ching-Ju Tsai, Anton Barty, Mark S Hunter, Nadia A Zatsepin, Celestino Padeste, Guido Capitani, W Henry Benner, Sébastien Boutet, Stefan P Hau-Riege and 13 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in IUCrJ, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Strategies for sample delivery for femtosecond crystallography.Acta crystallographica. Section D, Structural biology · 2019
    Review
  3. 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

23 authors.

Cecilia M CasadeiPaul Scherrer Institute, 5232 Villigen PSI, Switzerland.
Ching-Ju TsaiPaul Scherrer Institute, 5232 Villigen PSI, Switzerland.
Anton BartyCenter for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany.
Mark S HunterLawrence Livermore National Laboratory, 7000 East Avenue, Livermore, CA 94550, USA.
Nadia A ZatsepinArizona State University, 300 East University Drive, Tempe, AZ 85287, USA.
Celestino PadestePaul Scherrer Institute, 5232 Villigen PSI, Switzerland.ORCID https://orcid.org/0000-0001-7577-5781
Guido CapitaniPaul Scherrer Institute, 5232 Villigen PSI, Switzerland.
W Henry BennerLawrence Livermore National Laboratory, 7000 East Avenue, Livermore, CA 94550, USA.
Sébastien BoutetLinac Coherent Light Source, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.ORCID https://orcid.org/0000-0003-3928-1244
Stefan P Hau-RiegeLawrence Livermore National Laboratory, 7000 East Avenue, Livermore, CA 94550, USA.
Christopher KupitzArizona State University, 300 East University Drive, Tempe, AZ 85287, USA.
Marc MesserschmidtLinac Coherent Light Source, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.ORCID https://orcid.org/0000-0002-8641-3302
John I OgrenPhysics Departement, Boston University, 590 Commonwealth Avenue, Boston, MA 02215, USA.
Tom PardiniLawrence Livermore National Laboratory, 7000 East Avenue, Livermore, CA 94550, USA.
Kenneth J RothschildPhysics Departement, Boston University, 590 Commonwealth Avenue, Boston, MA 02215, USA.
Leonardo SalaPaul Scherrer Institute, 5232 Villigen PSI, Switzerland.
Brent SegelkeLawrence Livermore National Laboratory, 7000 East Avenue, Livermore, CA 94550, USA.
Garth J WilliamsLinac Coherent Light Source, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.
James E EvansEnvironmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, 3335 Innovation Boulevard, Richland, WA 99354, USA.
Xiao-Dan LiPaul Scherrer Institute, 5232 Villigen PSI, Switzerland.
Matthew ColemanLawrence Livermore National Laboratory, 7000 East Avenue, Livermore, CA 94550, USA.
Bill PedriniPaul Scherrer Institute, 5232 Villigen PSI, Switzerland.
Matthias FrankLawrence Livermore National Laboratory, 7000 East Avenue, Livermore, CA 94550, USA.

Funding

Technology development for biological imaging with x-ray free electron lasersR01GM117342 · NIGMS · LAWRENCE LIVERMORE NATIONAL SECURITY, LLC · PI FRANK, MATTHIAS · 2016 to 2024
$4.8M
NIGMS NIH HHS R01 GM117342
6 · The paper itself

Abstract

Previous proof-of-concept measurements on single-layer two-dimensional membrane-protein crystals performed at X-ray free-electron lasers (FELs) have demonstrated that the collection of meaningful diffraction patterns, which is not possible at synchrotrons because of radiation-damage issues, is feasible. Here, the results obtained from the analysis of a thousand single-shot, room-temperature X-ray FEL diffraction images from two-dimensional crystals of a bacteriorhodopsin mutant are reported in detail. The high redundancy in the measurements boosts the intensity signal-to-noise ratio, so that the values of the diffracted intensities can be reliably determined down to the detector-edge resolution of 4 Å. The results show that two-dimensional serial crystallography at X-ray FELs is a suitable method to study membrane proteins to near-atomic length scales at ambient temperature. The method presented here can be extended to pump-probe studies of optically triggered structural changes on submillisecond timescales in two-dimensional crystals, which allow functionally relevant large-scale motions that may be quenched in three-dimensional crystals.

Indexed as

free-electron lasersmembrane proteinsserial crystallographytwo-dimensional crystals

Identifiers

PMID29354276
PMCPMC5755582

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.