Evidence map›Paper›PMID 35938521›Full record

ArticleFaraday discussions2022

Application of super-resolution and correlative double sampling in cryo-electron microscopy.

Yuewen Sheng, Peter J Harrison, Vinod Vogirala, Zhengyi Yang, Claire Strain-Damerell, Thomas Frosio, Benjamin A Himes, C Alistair Siebert, Peijun Zhang, Daniel K Clare

Abstract read
In one paragraph

Article in Faraday discussions, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. 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

10 authors.

Yuewen ShengDiamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK. daniel.clare@diamond.ac.uk.ORCID 0000-0003-3067-9520
Peter J HarrisonDiamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK. daniel.clare@diamond.ac.uk.ORCID 0000-0001-5167-0547
Vinod VogiralaDiamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK. daniel.clare@diamond.ac.uk.
Zhengyi YangDiamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK. daniel.clare@diamond.ac.uk.ORCID 0000-0001-7190-7505
Claire Strain-DamerellDiamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK. daniel.clare@diamond.ac.uk.ORCID 0000-0003-4964-2090
Thomas FrosioDiamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK. daniel.clare@diamond.ac.uk.
Benjamin A HimesHoward Hughes Medical Institute, RNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, MA, USA.
C Alistair SiebertDiamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK. daniel.clare@diamond.ac.uk.
Peijun ZhangDiamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK. daniel.clare@diamond.ac.uk.ORCID 0000-0003-1803-691X
Daniel K ClareDiamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK. daniel.clare@diamond.ac.uk.ORCID 0000-0002-3372-8378

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CALERO, GUILLERMO ALBERTO · 2007 to 2018
$48.1M
Structure and function of membrane receptor signaling complex in bacterial chemotR01GM085043 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ZHANG, PEIJUN · 2009 to 2013
$1.4M
Cryo-FIB processing of vitreous biological specimen for electron tomographyR21RR024424 · NCRR · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ZHANG, PEIJUN · 2009 to 2010
$546k
Biotechnology and Biological Sciences Research CouncilMedical Research CouncilNCRR NIH HHS R21 RR024424NIGMS NIH HHS P50 GM082251NIGMS NIH HHS R01 GM085043Wellcome Trust
6 · The paper itself

Abstract

Developments in cryo-EM have allowed atomic or near-atomic resolution structure determination to become routine in single particle analysis (SPA). However, near-atomic resolution structures determined using cryo-electron tomography and sub-tomogram averaging (cryo-ET STA) are much less routine. In this paper, we show that collecting cryo-ET STA data using the same conditions as SPA, with both correlated double sampling (CDS) and the super-resolution mode, allowed apoferritin to be reconstructed out to the physical Nyquist frequency of the images. Even with just two tilt series, STA yields an apoferritin map at 2.9 Å resolution. These results highlight the exciting potential of cryo-ET STA in the future of protein structure determination. While processing SPA data recorded in super-resolution mode may yield structures surpassing the physical Nyquist limit, processing cryo-ET STA data in the super-resolution mode gave no additional resolution benefit. We further show that collecting SPA data in the super-resolution mode, with CDS activated, reduces the estimated

Indexed as

ApoferritinsElectron Microscope TomographyCryoelectron MicroscopyProteinsApoferritinsProteins

Identifiers

PMID35938521
PMCPMC9642007

What OpenQuestion holds

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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.