Evidence map›Paper›PMID 24914151›Full record

ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2014

Transmission electron microscopy as a tool for nanocrystal characterization pre- and post-injector.

H P Stevenson, D P DePonte, A M Makhov, James F Conway, O B Zeldin, S Boutet, G Calero, A E Cohen

Open access · bronzeAbstract read
In one paragraph

Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Structural basis of transcription: RNA polymerase II substrate binding and metal coordination using a free-electron laser.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Detection of Microcrystals for CryoEM.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  3. Article
  4. Strategies for sample delivery for femtosecond crystallography.Acta crystallographica. Section D, Structural biology · 2019
    Review
  5. Article
  6. Review
  7. Review
  8. Transmission electron microscopy for the evaluation and optimization of crystal growth.Acta crystallographica. Section D, Structural biology · 2016
    Article
  9. Article
  10. Article
  11. Raster-scanning serial protein crystallography using micro- and nano-focused synchrotron beams.Acta crystallographica. Section D, Biological crystallography · 2015
    Article
  12. Capture and X-ray diffraction studies of protein microcrystals in a microfluidic trap array.Acta crystallographica. Section D, Biological crystallography · 2015
    Article
  13. Goniometer-based femtosecond crystallography with X-ray free electron lasers.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  14. The birth of a new field.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014
    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

8 authors at 5 institutions in 1 country.

H P StevensonDepartment of Structural Biology, University of Pittsburgh School of Medicine, 1040 Biomedical Science Tower 3, Pittsburgh, PA 15260, USA.
D P DePonteLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.
A M MakhovDepartment of Structural Biology, University of Pittsburgh School of Medicine, 1040 Biomedical Science Tower 3, Pittsburgh, PA 15260, USA.
James F ConwayDepartment of Structural Biology, University of Pittsburgh School of Medicine, 1040 Biomedical Science Tower 3, Pittsburgh, PA 15260, USA.
O B ZeldinDepartment of Structural Biology and Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305, USA.
S BoutetLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.
G CaleroDepartment of Structural Biology, University of Pittsburgh School of Medicine, 1040 Biomedical Science Tower 3, Pittsburgh, PA 15260, USA gcalero@structbio.pitt.edu.
A E CohenStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, 2575 Sand Hill Road, Menlo Park, CA 94025, USA acohen@slac.stanford.edu.
University of Pittsburgh · USHoward Hughes Medical Institute · USLinac Coherent Light Source · USSLAC National Accelerator Laboratory · USStanford University · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393
6 · The paper itself

Abstract

Recent advancements at the Linac Coherent Light Source X-ray free-electron laser (XFEL) enabling successful serial femtosecond diffraction experiments using nanometre-sized crystals (NCs) have opened up the possibility of X-ray structure determination of proteins that produce only submicrometre crystals such as many membrane proteins. Careful crystal pre-characterization including compatibility testing of the sample delivery method is essential to ensure efficient use of the limited beamtime available at XFEL sources. This work demonstrates the utility of transmission electron microscopy for detecting and evaluating NCs within the carrier solutions of liquid injectors. The diffraction quality of these crystals may be assessed by examining the crystal lattice and by calculating the fast Fourier transform of the image. Injector reservoir solutions, as well as solutions collected post-injection, were evaluated for three types of protein NCs (i) the membrane protein PTHR1, (ii) the multi-protein complex Pol II-GFP and (iii) the soluble protein lysozyme. Our results indicate that the concentration and diffraction quality of NCs, particularly those with high solvent content and sensitivity to mechanical manipulation may be affected by the delivery process.

Indexed as

ElectronsLasersMolecular ConformationFourier AnalysisHumansMicroscopy, Electron, TransmissionMuramidaseNanoparticlesReceptor, Parathyroid Hormone, Type 1RNA Polymerase IIX-Ray DiffractionMuramidasePTH1R protein, humanReceptor, Parathyroid Hormone, Type 1RNA Polymerase IIcrystal characterizationcrystal injectorcrystallographyfemtosecond diffractionsample deliverytransmission electron microscopy (TEM)

Identifiers

PMID24914151
PMCPMC4052860
OpenAlexW2038232199

What OpenQuestion holds

Textmetadata
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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.