Evidence map›Paper›PMID 42689445›Full record

ReviewIUCrJ2026

A discussion of cryo-EM terminology as the outreach and number of PDB entries expand.

Bruno P Klaholz

Abstract readReview
In one paragraph

Review in IUCrJ, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

1 author.

Bruno P KlaholzCentre for Integrative Biology (CBI), Department of Integrated Structural Biology, IGBMC (Institute of Genetics and of Molecular and Cellular Biology), 1 rue Laurent Fries, Illkirch, France.ORCID 0000-0001-8674-8674

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cryo electron microscopy (cryo-EM) has made great advances in the last decade, progressively increasing its impact in structural biology as a key method to address molecular structures and mechanisms of various macromolecular complexes. Single-particle cryo-EM will soon equal the number of yearly entries in the Protein Data Bank from structures determined by X-ray crystallography. This is largely thanks to improved cryo electron microscope instrumentation and advanced image-processing tools and structure-sorting methods. As the role of cryo-EM is expanding to an increasingly large community, including newcomers and scientists joining from related fields, it is timely to revisit some fundamental concepts and basics of single-particle cryo-EM and image processing as terminology has become less well defined and, in some cases, confusing. Here we summarize and define some typical terms important for understanding the underlying physical concepts. These include `cryo-EM', `cryo-ET', `3D reconstruction', `coarsening', `contour level' and others. We also discuss resolution estimation and map deposition.

Indexed as

Cryoelectron MicroscopyDatabases, ProteinTerminology as TopicCrystallography, X-RayImage Processing, Computer-AssistedImaging, Three-Dimensional3D reconstruction and image processingcryo-EMcryo-ETPDBProtein Data Bank

Identifiers

PMID42689445
PMCPMC13548831

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.