Evidence map›Paper›PMID 24872454›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Use of transmission electron microscopy to identify nanocrystals of challenging protein targets.

Hilary P Stevenson, Alexander M Makhov, Monica Calero, Andrea L Edwards, Oliver B Zeldin, Irimpan I Mathews, Guowu Lin, Christopher O Barnes, Hugo Santamaria, Ted M Ross and 6 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. 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
  6. Reaching the potential of electron diffraction.Cell reports. Physical science · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Macromolecular crystallography using microcrystal electron diffraction.Acta crystallographica. Section D, Structural biology · 2021
    Review
  14. MicroED Sample Preparation and Data Collection For Protein Crystals.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  15. Detection of Microcrystals for CryoEM.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  16. Rapid screening ofJournal of applied crystallography · 2020
    Article
  17. Review
  18. Review
  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

16 authors.

Hilary P StevensonDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261;
Alexander M MakhovDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261;
Monica CaleroDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261;
Andrea L EdwardsDepartments of Chemical Engineering and Chemistry.
Oliver B ZeldinDepartment of Structural Biology, andHoward Hughes Medical Institute, Stanford University, Stanford, CA 94305;
Irimpan I MathewsStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025;
Guowu LinDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261;
Christopher O BarnesDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261;
Hugo SantamariaDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261;
Ted M RossVaccine and Gene Therapy Institute of Florida, Port St. Lucie, FL 34987; and.
S Michael SoltisStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025;
Chaitan KhoslaDepartments of Chemical Engineering and Chemistry.
V NagarajanJAN Scientific, Inc., Seattle, WA 98105.
James F ConwayDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261;
Aina E CohenStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025; acohen@slac.stanford.edu guc9@pitt.edu.
Guillermo CaleroDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261; acohen@slac.stanford.edu guc9@pitt.edu.

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Structure, Mechanism, and Engineering of Assembly Line Polyketide SynthasesR01GM087934 · NIGMS · STANFORD UNIVERSITY · PI KHOSLA, CHAITAN · 2009 to 2021
$4.9M
Howard Hughes Medical InstituteNIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393NIGMS NIH HHS R01 GM087934
6 · The paper itself

Abstract

The current practice for identifying crystal hits for X-ray crystallography relies on optical microscopy techniques that are limited to detecting crystals no smaller than 5 μm. Because of these limitations, nanometer-sized protein crystals cannot be distinguished from common amorphous precipitates, and therefore go unnoticed during screening. These crystals would be ideal candidates for further optimization or for femtosecond X-ray protein nanocrystallography. The latter technique offers the possibility to solve high-resolution structures using submicron crystals. Transmission electron microscopy (TEM) was used to visualize nanocrystals (NCs) found in crystallization drops that would classically not be considered as "hits." We found that protein NCs were readily detected in all samples tested, including multiprotein complexes and membrane proteins. NC quality was evaluated by TEM visualization of lattices, and diffraction quality was validated by experiments in an X-ray free electron laser.

Indexed as

AnimalsCrystallizationCrystallography, X-RayEscherichia coliMicroscopy, Electron, TransmissionNanoparticlesProteinsRecombinant ProteinsReproducibility of ResultsSf9 CellsProteinsRecombinant Proteinscrystal characterizationcrystal optimizationfemtosecond diffractionnanocrystal detectionstructural biology

Identifiers

PMID24872454
PMCPMC4060711

What OpenQuestion holds

Textmetadata
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.