Evidence map›Paper›PMID 31292253›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Microfluidic protein isolation and sample preparation for high-resolution cryo-EM.

Claudio Schmidli, Stefan Albiez, Luca Rima, Ricardo Righetto, Inayatulla Mohammed, Paolo Oliva, Lubomir Kovacik, Henning Stahlberg, Thomas Braun

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
6.3field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. VitroJet: new features and case studies.Acta crystallographica. Section D, Structural biology · 2024
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022
    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

9 authors at 1 institution in 1 country.

Claudio SchmidliCenter for Cellular Imaging and Nanoanalytics, Biozentrum, 4058 Basel, Switzerland.
Stefan AlbiezCenter for Cellular Imaging and Nanoanalytics, Biozentrum, 4058 Basel, Switzerland.
Luca RimaCenter for Cellular Imaging and Nanoanalytics, Biozentrum, 4058 Basel, Switzerland.
Ricardo RighettoCenter for Cellular Imaging and Nanoanalytics, Biozentrum, 4058 Basel, Switzerland.
Inayatulla MohammedCenter for Cellular Imaging and Nanoanalytics, Biozentrum, 4058 Basel, Switzerland.
Paolo OlivaCenter for Cellular Imaging and Nanoanalytics, Biozentrum, 4058 Basel, Switzerland.
Lubomir KovacikCenter for Cellular Imaging and Nanoanalytics, Biozentrum, 4058 Basel, Switzerland.
Henning StahlbergCenter for Cellular Imaging and Nanoanalytics, Biozentrum, 4058 Basel, Switzerland.ORCID 0000-0002-1185-4592
Thomas BraunCenter for Cellular Imaging and Nanoanalytics, Biozentrum, 4058 Basel, Switzerland; thomas.braun@unibas.ch.ORCID 0000-0002-9148-0200
University of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High-resolution structural information is essential to understand protein function. Protein-structure determination needs a considerable amount of protein, which can be challenging to produce, often involving harsh and lengthy procedures. In contrast, the several thousand to a few million protein particles required for structure determination by cryogenic electron microscopy (cryo-EM) can be provided by miniaturized systems. Here, we present a microfluidic method for the rapid isolation of a target protein and its direct preparation for cryo-EM. Less than 1 μL of cell lysate is required as starting material to solve the atomic structure of the untagged, endogenous human 20S proteasome. Our work paves the way for high-throughput structure determination of proteins from minimal amounts of cell lysate and opens more opportunities for the isolation of sensitive, endogenous protein complexes.

Indexed as

BiotinylationCryoelectron MicroscopyHeLa CellsHumansImage Processing, Computer-AssistedImaging, Three-DimensionalImmunoglobulin Fab FragmentsMicrofluidic Analytical TechniquesProteasome Endopeptidase ComplexProtein ConformationProtein SubunitsVitrificationImmunoglobulin Fab FragmentsProteasome Endopeptidase ComplexProtein Subunitscryo-EMendogenousmicrofluidicsprotein purificationsample preparation

Identifiers

PMID31292253
PMCPMC6660723
OpenAlexW2959223248

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.