Evidence map›Paper›PMID 33217329›Full record

ArticleStructure (London, England : 1993)2021

Native Mass Spectrometry-Based Screening for Optimal Sample Preparation in Single-Particle Cryo-EM.

Paul Dominic B Olinares, Jin Young Kang, Eliza Llewellyn, Courtney Chiu, James Chen, Brandon Malone, Ruth M Saecker, Elizabeth A Campbell, Seth A Darst, Brian T Chait

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Computed Vibrational Heat Capacities for Gas-Phase Biomolecular Ions.Journal of the American Society for Mass Spectrometry · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Mass spectrometers as cryoEM grid preparation instruments.Current opinion in structural biology · 2023
    Review
  11. Dissecting the structural heterogeneity of proteins by native mass spectrometry.Protein science : a publication of the Protein Society · 2023
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Review
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 at 1 institution in 1 country.

Paul Dominic B OlinaresLaboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065, USA. Electronic address: paul.olinares@rockefeller.edu.
Jin Young KangLaboratory of Molecular Biophysics, The Rockefeller University, New York, NY 10065, USA.
Eliza LlewellynLaboratory of Molecular Biophysics, The Rockefeller University, New York, NY 10065, USA.
Courtney ChiuLaboratory of Molecular Biophysics, The Rockefeller University, New York, NY 10065, USA.
James ChenLaboratory of Molecular Biophysics, The Rockefeller University, New York, NY 10065, USA.
Brandon MaloneLaboratory of Molecular Biophysics, The Rockefeller University, New York, NY 10065, USA.
Ruth M SaeckerLaboratory of Molecular Biophysics, The Rockefeller University, New York, NY 10065, USA.
Elizabeth A CampbellLaboratory of Molecular Biophysics, The Rockefeller University, New York, NY 10065, USA.
Seth A DarstLaboratory of Molecular Biophysics, The Rockefeller University, New York, NY 10065, USA.
Brian T ChaitLaboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065, USA. Electronic address: chait@rockefeller.edu.
Rockefeller University · US

Funding

NCCAT: National Center for CryoEM Access and Training- Supplement for Windows 10 and FFIU24GM129539 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2018 to 2023
$53.9M
TR&D Project 4. The Imaging Stage: Multiscale Spatiotemporal Modeling of Macromolecular Systems in Cellular NeighborhoodsP41GM109824 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2014 to 2023
$18.8M
TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
National Resource for Mass Spectrom of Biological MacromoleculesP41GM103314 · NIGMS · ROCKEFELLER UNIVERSITY · PI CHAIT, BRIAN T · 2012 to 2017
$9.9M
Structure, function, and regulation of the bacterial transcription cycleR35GM118130 · NIGMS · ROCKEFELLER UNIVERSITY · PI DARST, SETH A. · 2016 to 2025
$8.9M
Structure, function, and inhibition of the SARS-CoV-2 replication-transcription complexR01AI161278 · NIAID · ROCKEFELLER UNIVERSITY · PI Seth A. Darst · 2021 to 2026
$3.9M
Structure/function analyses of essential mycobacterial transcription regulatorsR01GM114450 · NIGMS · ROCKEFELLER UNIVERSITY · PI CAMPBELL, ELIZABETH A · 2015 to 2023
$3.4M
NIAID NIH HHS R01 AI161278NIGMS NIH HHS P41 GM103310NIGMS NIH HHS P41 GM103314NIGMS NIH HHS P41 GM109824NIGMS NIH HHS R01 GM114450NIGMS NIH HHS R35 GM118130NIGMS NIH HHS U24 GM129539
6 · The paper itself

Abstract

Recent advances in single-particle cryogenic electron microscopy (cryo-EM) have enabled the structural determination of numerous protein assemblies at high resolution, yielding unprecedented insights into their function. However, despite its extraordinary capabilities, cryo-EM remains time-consuming and resource-intensive. It is therefore beneficial to have a means for rapidly assessing and optimizing the quality of samples prior to lengthy cryo-EM analyses. To do this, we have developed a native mass spectrometry (nMS) platform that provides rapid feedback on sample quality and highly streamlined biochemical screening. Because nMS enables accurate mass analysis of protein complexes, it is well suited to routine evaluation of the composition, integrity, and homogeneity of samples prior to their plunge-freezing on EM grids. We demonstrate the utility of our nMS-based platform for facilitating cryo-EM studies using structural characterizations of exemplar bacterial transcription complexes as well as the replication-transcription assembly from the SARS-CoV-2 virus that is responsible for the COVID-19 pandemic.

Indexed as

Cryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsMass SpectrometryMethyltransferasesRNA HelicasesSARS-CoV-2Single Molecule ImagingTranscription FactorsViral Nonstructural ProteinsEscherichia coli ProteinsMethyltransferasesNsp13 protein, SARS-CoVRNA HelicasesTranscription FactorsTraR protein, E coliViral Nonstructural Proteinsbacterial RNA polymerasebiochemical screeningcryo-EMcryo-EM sample quality checkintegrated structural biologynative mass spectrometryprotein complexesSARS-CoV-2 replication-transcription complextranscription

Identifiers

PMID33217329
PMCPMC7867593
OpenAlexW3101753867

What OpenQuestion holds

Textmetadata
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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.