Evidence map›Paper›PMID 42275466›Full record

ArticleScience (New York, N.Y.)2026

Laser phase plate improves structure determination of small proteins by cryo-EM.

Petar N Petrov, Jessie T Zhang, Jonathan Remis, Jeremy J Axelrod, Hang Cheng, Eric S Cooper, Ian K Hicklin, Shahar Sandhaus, Cooper Schnurr, Robert M Glaeser and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science (New York, N.Y.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

11 authors.

Petar N Petrov *Department of Physics, University of California, Berkeley, Berkeley, CA, USA.ORCID 0000-0002-3806-534X
Jessie T Zhang *Department of Physics, University of California, Berkeley, Berkeley, CA, USA.ORCID 0000-0002-0202-1222
Jonathan RemisDepartment of Physics, University of California, Berkeley, Berkeley, CA, USA.ORCID 0000-0001-8317-4513
Jeremy J AxelrodDepartment of Physics, University of California, Berkeley, Berkeley, CA, USA.ORCID 0000-0003-3564-241X
Hang ChengDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, USA.ORCID 0009-0007-3236-9872
Eric S CooperDepartment of Physics, University of California, Berkeley, Berkeley, CA, USA.ORCID 0000-0002-8620-4252
Ian K HicklinDepartment of Physics, University of California, Berkeley, Berkeley, CA, USA.ORCID 0009-0009-0436-8981
Shahar SandhausDepartment of Physics, University of California, Berkeley, Berkeley, CA, USA.ORCID 0009-0002-9822-8929
Cooper SchnurrDepartment of Physics, University of California, Berkeley, Berkeley, CA, USA.ORCID 0009-0009-5296-8025
Robert M GlaeserLawrence Berkeley National Laboratory, Berkeley, CA, USA.ORCID 0000-0003-1955-1825
Holger MüllerDepartment of Physics, University of California, Berkeley, Berkeley, CA, USA.ORCID 0000-0003-0636-5951

Funding

Development of Laser-Based Phase Contrast for Biological Electron MicroscopyR01GM126011 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI MUELLER, HOLGER · 2017 to 2024
$3.9M
Investigating MHC-I downregulation by HIV-1 Nef using cryo-electron tomography with laser-based phase contrastF32GM149186 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI PETROV, PETAR NIKOLOV · 2023 to 2023
$70k
NIGMS NIH HHS F32 GM149186NIGMS NIH HHS R01 GM126011
6 · The paper itself

Abstract

Phase plates can, in principle, overcome the poor image contrast in cryo-electron microscopy (cryo-EM) and the resulting limits on the structural reconstruction of small proteins. However, previous designs have been unstable and compromised the high-resolution signal and have thus been unable to surpass results achieved by standard cryo-EM. Here, we show that the laser phase plate (LPP), installed in a modern, custom Titan Krios microscope, enhances the resolution in single-particle reconstruction of small proteins by improving specimen-motion correction and recovery of information from the early frames, as well as particle visualization, three-dimensional classification, and alignment. These advances use standard defocus ranges and reconstruction procedures but open the door to LPP-tailored protocols, offering further improvements by leveraging the LPP demonstrated here.

Indexed as

Cryoelectron MicroscopyLasersProteinsImaging, Three-DimensionalProtein ConformationProteins

Identifiers

PMID42275466
PMCPMC13633750

What OpenQuestion holds

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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.