Evidence map›Paper›PMID 27647903›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Ab initio structure determination from prion nanocrystals at atomic resolution by MicroED.

Michael R Sawaya, Jose Rodriguez, Duilio Cascio, Michael J Collazo, Dan Shi, Francis E Reyes, Johan Hattne, Tamir Gonen, David S Eisenberg

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing 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

66 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. 3D Nanocrystallography and the Imperfect Molecular Lattice.Annual review of physical chemistry · 2024
    Review
  7. Article
  8. Article
  9. Fragment-BasedACS bio & med chem Au · 2023
    Article
  10. MicroED in drug discovery.Current opinion in structural biology · 2023
    Review
  11. Design and implementation of suspended drop crystallization.bioRxiv : the preprint server for biology · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Studying membrane proteins with MicroED.Biochemical Society transactions · 2022
    Article
  20. Article

6 more citing papers are in PubMed but not listed here.

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

9 authors.

Michael R SawayaHoward Hughes Medical Institute, University of California, Los Angeles, CA 90024-1570; University of California, Los Angeles-Department of Energy Institute, University of California, Los Angeles, CA 90024-1570; Department of Biological Chemistry, University of California, Los Angeles, CA 90024-1570; Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024-1570; Molecular Biology Institute, University of California, Los Angeles, CA 90024-1570.
Jose RodriguezHoward Hughes Medical Institute, University of California, Los Angeles, CA 90024-1570; University of California, Los Angeles-Department of Energy Institute, University of California, Los Angeles, CA 90024-1570; Department of Biological Chemistry, University of California, Los Angeles, CA 90024-1570; Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024-1570; Molecular Biology Institute, University of California, Los Angeles, CA 90024-1570.
Duilio CascioHoward Hughes Medical Institute, University of California, Los Angeles, CA 90024-1570; University of California, Los Angeles-Department of Energy Institute, University of California, Los Angeles, CA 90024-1570; Department of Biological Chemistry, University of California, Los Angeles, CA 90024-1570; Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024-1570; Molecular Biology Institute, University of California, Los Angeles, CA 90024-1570.
Michael J CollazoHoward Hughes Medical Institute, University of California, Los Angeles, CA 90024-1570; University of California, Los Angeles-Department of Energy Institute, University of California, Los Angeles, CA 90024-1570; Department of Biological Chemistry, University of California, Los Angeles, CA 90024-1570; Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024-1570; Molecular Biology Institute, University of California, Los Angeles, CA 90024-1570.
Dan ShiHoward Hughes Medical Institute, Janelia Research Campus, Ashburn, VA 20147.
Francis E ReyesHoward Hughes Medical Institute, Janelia Research Campus, Ashburn, VA 20147.
Johan HattneHoward Hughes Medical Institute, Janelia Research Campus, Ashburn, VA 20147.ORCID 0000-0002-8936-0912
Tamir GonenHoward Hughes Medical Institute, Janelia Research Campus, Ashburn, VA 20147 gonent@janelia.hhmi.org david@mbi.ucla.edu.
David S EisenbergHoward Hughes Medical Institute, University of California, Los Angeles, CA 90024-1570; University of California, Los Angeles-Department of Energy Institute, University of California, Los Angeles, CA 90024-1570; Department of Biological Chemistry, University of California, Los Angeles, CA 90024-1570; Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024-1570; Molecular Biology Institute, University of California, Los Angeles, CA 90024-1570; gonent@janelia.hhmi.org david@mbi.ucla.edu.

Funding

Structural Biology of Amyloid DiseaseR01AG029430 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI EISENBERG, DAVID · 2007 to 2016
$3.9M
Howard Hughes Medical InstituteNIA NIH HHS R01 AG029430
6 · The paper itself

Abstract

Electrons, because of their strong interaction with matter, produce high-resolution diffraction patterns from tiny 3D crystals only a few hundred nanometers thick in a frozen-hydrated state. This discovery offers the prospect of facile structure determination of complex biological macromolecules, which cannot be coaxed to form crystals large enough for conventional crystallography or cannot easily be produced in sufficient quantities. Two potential obstacles stand in the way. The first is a phenomenon known as dynamical scattering, in which multiple scattering events scramble the recorded electron diffraction intensities so that they are no longer informative of the crystallized molecule. The second obstacle is the lack of a proven means of de novo phase determination, as is required if the molecule crystallized is insufficiently similar to one that has been previously determined. We show with four structures of the amyloid core of the Sup35 prion protein that, if the diffraction resolution is high enough, sufficiently accurate phases can be obtained by direct methods with the cryo-EM method microelectron diffraction (MicroED), just as in X-ray diffraction. The success of these four experiments dispels the concern that dynamical scattering is an obstacle to ab initio phasing by MicroED and suggests that structures of novel macromolecules can also be determined by direct methods.

Indexed as

Models, MolecularX-Ray DiffractionAmino Acid SequenceAmyloidComputer SimulationCrystallography, X-RayHydrogenNanoparticlesPrionsAmyloidHydrogenPrionselectron diffractionMicroEDnanocrystalphasingprion

Identifiers

PMID27647903
PMCPMC5056061

What OpenQuestion holds

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Registered trials

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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.