Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

3.3K
Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
3.3K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

DAQplugin: Deep Learning based Real-time Model Evaluation Plugin for ChimeraX.

bioRxiv : the preprint server for biology·2026
Same author

A generalizable Hi-C foundation model for chromatin architecture, single-cell and multiomics analysis across species.

Nature methods·2026
Same author

Direct Detection and Atomic Modeling of Ligands in Cryo-EM Maps Using Deep Learning.

bioRxiv : the preprint server for biology·2026
Same author

On the state of protein function prediction: a report on the fourth CAFA challenge.

bioRxiv : the preprint server for biology·2026
Same author

PL-PatchSurfer3: improved structure-based virtual screening for structure variation using 3D Zernike descriptors.

Journal of cheminformatics·2026
Same author

Multivalent recognition of ferritin by full-length NCOA4 enables robust ferritinophagy.

Protein science : a publication of the Protein Society·2026
Same journal

Layered social competition coordinates reproductive hierarchy formation in ants.

bioRxiv : the preprint server for biology·2026
Same journal

Combination epigenetic-targeted therapy increases the immunogenicity of poorly immunogenic sarcomas.

bioRxiv : the preprint server for biology·2026
Same journal

Loss of LanC-like proteins delays post-injury regeneration of aging skeletal muscles.

bioRxiv : the preprint server for biology·2026
Same journal

Integrative Transfer Network: Deep Transfer Learning Across Populations and Prediction Targets.

bioRxiv : the preprint server for biology·2026
Same journal

Confidence-supported label-free metabolic imaging with FPhaS phase autofluorescence microscopy.

bioRxiv : the preprint server for biology·2026
Same journal

Sequence-encoded autoinhibition couples mRNA decapping activity to phase separation.

bioRxiv : the preprint server for biology·2026
See all related articles

Related Experiment Video

Updated: Jul 4, 2025

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
09:30

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

1.3K

DiffModeler: Large Macromolecular Structure Modeling in Low-Resolution Cryo-EM Maps Using Diffusion Model.

Xiao Wang1, Han Zhu1, Genki Terashi2

  • 1Department of Computer Science, Purdue University, West Lafayette, Indiana, 47907, USA.

Biorxiv : the Preprint Server for Biology
|February 8, 2024
PubMed
Summary
This summary is machine-generated.

DiffModeler, an automated method, accurately models complex protein structures from intermediate-resolution cryo-electron microscopy (cryo-EM) maps. It integrates diffusion models and AlphaFold2 predictions, achieving high accuracy even for large complexes.

More Related Videos

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
09:25

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction

Published on: January 9, 2015

46.2K
Single Particle Cryo-Electron Microscopy: From Sample to Structure
11:52

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

8.5K

Related Experiment Videos

Last Updated: Jul 4, 2025

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
09:30

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

1.3K
Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
09:25

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction

Published on: January 9, 2015

46.2K
Single Particle Cryo-Electron Microscopy: From Sample to Structure
11:52

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

8.5K

Area of Science:

  • Structural biology
  • Computational biology
  • Biophysics

Background:

  • Cryo-electron microscopy (cryo-EM) is crucial for determining multi-chain protein complex structures.
  • Modeling protein complexes at intermediate resolutions (5-10 Å) remains a significant challenge.
  • Existing methods struggle with accurate structure fitting and de novo modeling in this resolution range.

Approach:

  • Introduces DiffModeler, a fully automated method for protein complex structure modeling.
  • Employs a diffusion model for backbone tracing.
  • Integrates AlphaFold2-predicted single-chain structures for enhanced structure fitting.

Key Points:

  • DiffModeler achieves exceptional accuracy on intermediate-resolution cryo-EM maps, with an average TM-Score of 0.92.
  • Successfully modeled a 47-chain, 13,462-residue complex with a TM-Score of 0.94.
  • Demonstrates versatility at low resolutions (10-20 Å) and excels in protein-nucleic acid complex modeling with CryoREAD.

Conclusions:

  • DiffModeler significantly advances automated protein complex structure modeling, especially at intermediate resolutions.
  • Provides a robust solution for challenging cryo-EM data.
  • Shows potential for modeling large, complex biological assemblies and nucleic acid interactions.