Evidence map›Paper›PMID 36922493›Full record

ArticleNature communications2023

Determining protein structures in cellular lamella at pseudo-atomic resolution by GisSPA.

Jing Cheng, Tong Liu, Xin You, Fa Zhang, Sen-Fang Sui, Xiaohua Wan, Xinzheng Zhang

Erratum issuedOpen access · goldFull text read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
12.7field-weighted citation impact, top 2% 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

26 citing papers in PubMed, 46 citations in OpenAlex.

  1. eLife · 2026
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  12. Structural Basis of TACO1-Mediated Efficient Mitochondrial Translation.bioRxiv : the preprint server for biology · 2025
    Article
  13. Review
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  15. In situ structures of theProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Extending the reach of single-particle cryoEM.Current opinion in structural biology · 2025
    Review
  17. Review
  18. Capturing eukaryotic ribosome dynamics in situ at high resolution.Nature structural & molecular biology · 2025
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Jing Cheng *National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.ORCID http://orcid.org/0000-0002-3917-3756
Tong Liu *High Performance Computer Research Center, Institute of Computing Technology, Chinese Academy of Sciences, Beijing, 100190, China.
Xin YouState Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.ORCID http://orcid.org/0000-0002-9181-8646
Fa ZhangBeijing Institute of Technology, Beijing, 100081, China.
Sen-Fang SuiState Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.ORCID http://orcid.org/0000-0001-5253-2592
Xiaohua WanBeijing Institute of Technology, Beijing, 100081, China. wanxiaohua@bit.edu.cn.ORCID http://orcid.org/0000-0002-9340-878X
Xinzheng ZhangNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. xzzhang@ibp.ac.cn.ORCID http://orcid.org/0000-0002-0114-0270
Chinese Academy of Sciences · CNBeijing Institute of Technology · CNState Key Laboratory of Membrane Biology

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cryo-electron tomography is a major tool used to study the structure of protein complexes in situ. However, the throughput of tilt-series image data collection is still quite low. Here, we show that GisSPA, a GPU accelerated program, can translationally and rotationally localize the target protein complex in cellular lamellae, as prepared with a focused ion beam, using single cryo-electron microscopy images without tilt-series, and reconstruct the protein complex at near-atomic resolution. GisSPA allows high-throughput data collection without the acquisition of tilt-series images and reconstruction of the tomogram, which is essential for high-resolution reconstruction of asymmetric or low-symmetry protein complexes. We demonstrate the power of GisSPA with 3.4-Å and 3.9-Å resolutions of resolving phycobilisome and tetrameric photosystem II complex structures in cellular lamellae, respectively. In this work, we present GisSPA as a practical tool that facilitates high-resolution in situ protein structure determination.

Indexed as

Electron Microscope TomographyImage Processing, Computer-AssistedCryoelectron Microscopy

Identifiers

PMID36922493
PMCPMC10017804
OpenAlexW4324344460

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LicenceCC BY
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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.