Evidence map›Paper›PMID 39388715›Full record

ArticleJournal of the American Chemical Society2024

Exploring Transient States of PAmKate to Enable Improved Cryogenic Single-Molecule Imaging.

Davis Perez, Dara P Dowlatshahi, Christopher A Azaldegui, T Bertie Ansell, Peter D Dahlberg, W E Moerner

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Cryogenic electron tomography by the numbers: Charting underexplored lineages in structural cell biology.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Time-deterministic cryo-optical microscopy.Light, science & applications · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Davis PerezDepartment of Chemistry, Stanford University, Stanford, California 94305, United States.
Dara P DowlatshahiBiosciences Division, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.ORCID 0000-0002-6801-915X
Christopher A AzaldeguiDivision of CryoEM and Bioimaging, Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.
T Bertie AnsellDivision of CryoEM and Bioimaging, Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.
Peter D DahlbergDivision of CryoEM and Bioimaging, Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.ORCID 0000-0003-4452-2663
W E MoernerDepartment of Chemistry, Stanford University, Stanford, California 94305, United States.ORCID 0000-0002-2830-209X

Funding

Single-Molecule Imaging for Cell Biology and Super-Resolution MicroscopyR35GM118067 · NIGMS · STANFORD UNIVERSITY · PI MOERNER, WILLIAM E · 2016 to 2025
$6.2M
NIGMS NIH HHS R35 GM118067Wellcome Trust
6 · The paper itself

Abstract

Super-resolved cryogenic correlative light and electron microscopy is a powerful approach which combines the single-molecule specificity and sensitivity of fluorescence imaging with the nanoscale resolution of cryogenic electron tomography. Key to this method is active control over the emissive state of fluorescent labels to ensure sufficient sparsity to localize individual emitters. Recent work has identified fluorescent proteins (FPs) that photoactivate or photoswitch efficiently at cryogenic temperatures, but long on-times due to reduced quantum yield of photobleaching remain a challenge for imaging structures with a high density of localizations. In this work, we explore the photophysical properties of the red photoactivatable FP PAmKate and identify a 2-color process leading to enhanced turn-off of active emitters, improving localization rate. Specifically, after excitation of ground state molecules, we find that a transient state forms with a lifetime of ∼2 ms under cryogenic conditions, which can be bleached by exposure to a second wavelength. We measure the response of the transient state to different wavelengths, demonstrate how this mechanism can be used to improve imaging, and provide a blueprint for the study of other FPs at cryogenic temperatures.

Indexed as

Single Molecule ImagingCryoelectron MicroscopyFluorescent DyesLuminescent ProteinsFluorescent DyesLuminescent Proteins

Identifiers

PMID39388715
PMCPMC11505402

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.