Evidence map›Paper›PMID 33087927›Full record

ArticleNature2020

Atomic-resolution protein structure determination by cryo-EM.

Ka Man Yip, Niels Fischer, Elham Paknia, Ashwin Chari, Holger Stark

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 384 papers.

0numbers the graph read from it
0cells of the map it votes in
384citing papers in PubMed
68.1field-weighted citation impact, top 1% of its field
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

384 citing papers in PubMed, 767 citations in OpenAlex.

  1. Exchange dynamics and kinetic control of gene regulation complexes.Nature reviews. Molecular cell biology · 2026
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  16. 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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324 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Ka Man YipDepartment of Structural Dynamics, MPI for Biophysical Chemistry, Göttingen, Germany.
Niels FischerDepartment of Structural Dynamics, MPI for Biophysical Chemistry, Göttingen, Germany.ORCID http://orcid.org/0000-0002-4609-4052
Elham PakniaDepartment of Structural Dynamics, MPI for Biophysical Chemistry, Göttingen, Germany.
Ashwin ChariDepartment of Structural Dynamics, MPI for Biophysical Chemistry, Göttingen, Germany.ORCID http://orcid.org/0000-0001-6220-9828
Holger StarkDepartment of Structural Dynamics, MPI for Biophysical Chemistry, Göttingen, Germany. hstark1@gwdg.de.ORCID http://orcid.org/0000-0002-6161-1118
Max Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-particle electron cryo-microscopy (cryo-EM) is a powerful method for solving the three-dimensional structures of biological macromolecules. The technological development of transmission electron microscopes, detectors and automated procedures in combination with user-friendly image processing software and ever-increasing computational power have made cryo-EM a successful and expanding technology over the past decade

Indexed as

ApoferritinsCryoelectron MicroscopyDrug DesignHumansHydrogenModels, MolecularQuality ControlApoferritinsHydrogen

Identifiers

PMID33087927
OpenAlexW3094051077

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.