Evidence map›Paper›PMID 27572734›Full record

ReviewMethods in enzymology2016

High-Resolution Macromolecular Structure Determination by MicroED, a cryo-EM Method.

J A Rodriguez, T Gonen

Abstract readReview
In one paragraph

Review in Methods in enzymology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Studying Membrane Protein Structures by MicroED.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  3. Article
  4. Molecular engineering strategies for visualizing low-affinity protein complexes.Experimental biology and medicine (Maywood, N.J.) · 2019
    Article
  5. Article
  6. Taking the measure of MicroED.Current opinion in structural biology · 2017
    Review
  7. 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

2 authors.

J A RodriguezUCLA-DOE Institute, University of California, Los Angeles CA, United States.
T GonenJanelia Research Campus, Howard Hughes Medical Institute, Ashburn VA, United States. Electronic address: gonent@janelia.hhmi.org.

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Microelectron diffraction (MicroED) is a new cryo-electron microscopy (cryo-EM) method capable of determining macromolecular structures at atomic resolution from vanishingly small 3D crystals. MicroED promises to solve atomic resolution structures from even the tiniest of crystals, less than a few hundred nanometers thick. MicroED complements frontier advances in crystallography and represents part of the rebirth of cryo-EM that is making macromolecular structure determination more accessible for all. Here we review the concept and practice of MicroED, for both the electron microscopist and crystallographer. Where other reviews have addressed specific details of the technique (Hattne et al., 2015; Shi et al., 2016; Shi, Nannenga, Iadanza, & Gonen, 2013), we aim to provide context and highlight important features that should be considered when performing a MicroED experiment.

Indexed as

AlgorithmsSoftwareAnimalsCatalaseCattleCryoelectron MicroscopyCrystallographyFourier AnalysisImage Processing, Computer-AssistedImaging, Three-DimensionalLiverMicroscopy, Electron, TransmissionModels, MolecularMuramidaseCatalaseMuramidasecryo-EMCrystalCrystallographyDiffractionElectronMicroEDProtein

Identifiers

PMID27572734
PMCPMC5656567

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.