Evidence map›Paper›PMID 27572723›Full record

ReviewMethods in enzymology2016

Specimen Preparation for High-Resolution Cryo-EM.

L A Passmore, C J Russo

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 106 papers.

0numbers the graph read from it
0cells of the map it votes in
106citing 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

106 citing papers in PubMed.

  1. Article
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  7. Measurement of atomic scattering factors by cryoelectron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2026
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46 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

2 authors.

L A PassmoreMRC Laboratory of Molecular Biology, Cambridge, United Kingdom. Electronic address: passmore@mrc-lmb.cam.ac.uk.
C J RussoMRC Laboratory of Molecular Biology, Cambridge, United Kingdom. Electronic address: crusso@mrc-lmb.cam.ac.uk.

Funding

European Research Council 261151Medical Research Council MC_U105184326Medical Research Council MC_U105192715
6 · The paper itself

Abstract

Imaging a material with electrons at near-atomic resolution requires a thin specimen that is stable in the vacuum of the transmission electron microscope. For biological samples, this comprises a thin layer of frozen aqueous solution containing the biomolecular complex of interest. The process of preparing a high-quality specimen is often the limiting step in the determination of structures by single-particle electron cryomicroscopy (cryo-EM). Here, we describe a systematic approach for going from a purified biomolecular complex in aqueous solution to high-resolution electron micrographs that are suitable for 3D structure determination. This includes a series of protocols for the preparation of vitrified specimens on various supports, including all-gold and graphene. We also describe techniques for troubleshooting when a preparation fails to yield suitable specimens, and common mistakes to avoid during each part of the process. Finally, we include recommendations for obtaining the highest quality micrographs from prepared specimens with current microscope, detector, and support technology.

Indexed as

Cryoelectron MicroscopyEquipment DesignGoldGraphiteHumansImage Processing, Computer-AssistedProteinsSpecimen HandlingStaining and LabelingVitrificationGoldGraphiteProteinsCryo-EMElectron cryo-microscopyElectron tomographyProtein structureSingle-particle reconstructionSubstrates

Identifiers

PMID27572723
PMCPMC5140023

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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.