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

You might also read

Related Articles

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

Sort by
Same author

The amyloid packing difference: A pairwise comparison metric for amyloid structures.

Structure (London, England : 1993)·2026
Same author

Twelve phosphomimetic mutations induce the assembly of recombinant full-length human tau into paired helical filaments.

eLife·2026
Same author

Seeding biosensor cell line that reproduces the Alzheimer tau fold.

The Journal of biological chemistry·2025
Same author

Author Correction: Structures of α-synuclein filaments from multiple system atrophy.

Nature·2025
Same author

Seed structure and phosphorylation in the fuzzy coat impact tau seeding competency.

Nature communications·2025
Same author

Serial amplification of tau filaments using Alzheimer's brain homogenates and C322A or C322S recombinant tau.

FEBS letters·2025

Related Experiment Video

Updated: Dec 28, 2025

Use of Two Dimensional Semi-denaturing Detergent Agarose Gel Electrophoresis to Confirm Size Heterogeneity of Amyloid or Amyloid-like Fibers
10:10

Use of Two Dimensional Semi-denaturing Detergent Agarose Gel Electrophoresis to Confirm Size Heterogeneity of Amyloid or Amyloid-like Fibers

Published on: April 26, 2018

10.3K

Amyloid structure determination in RELION-3.1.

Sjors H W Scheres1

  • 1MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, England.

Acta Crystallographica. Section D, Structural Biology
|February 11, 2020
PubMed
Summary
This summary is machine-generated.

Determining atomic structures of amyloid filaments using electron cryo-microscopy (cryo-EM) is challenging due to local optima. This study introduces a new method in RELION to generate better initial models, simplifying amyloid structure determination.

Keywords:
Bayesian frameworkRELIONamyloidcryo-EMhelical reconstruction

More Related Videos

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
10:04

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

13.9K
Author Spotlight: Non-Invasive Imaging of Complex Bio-Structures Using Polarization-Sensitive Two-Photon Microscopy
05:54

Author Spotlight: Non-Invasive Imaging of Complex Bio-Structures Using Polarization-Sensitive Two-Photon Microscopy

Published on: September 8, 2023

1.6K

Related Experiment Videos

Last Updated: Dec 28, 2025

Use of Two Dimensional Semi-denaturing Detergent Agarose Gel Electrophoresis to Confirm Size Heterogeneity of Amyloid or Amyloid-like Fibers
10:10

Use of Two Dimensional Semi-denaturing Detergent Agarose Gel Electrophoresis to Confirm Size Heterogeneity of Amyloid or Amyloid-like Fibers

Published on: April 26, 2018

10.3K
Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
10:04

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

13.9K
Author Spotlight: Non-Invasive Imaging of Complex Bio-Structures Using Polarization-Sensitive Two-Photon Microscopy
05:54

Author Spotlight: Non-Invasive Imaging of Complex Bio-Structures Using Polarization-Sensitive Two-Photon Microscopy

Published on: September 8, 2023

1.6K

Area of Science:

  • Structural Biology
  • Biophysics
  • Neuroscience

Background:

  • Electron cryo-microscopy (cryo-EM) and helical reconstruction are key for atomic structure determination of amyloid filaments.
  • Amyloid structure determination is often hindered by local optima in the refinement process, complicating analysis.
  • RELION software is widely used for these analyses.

Purpose of the Study:

  • To assist users of RELION software in determining amyloid structures.
  • To address the challenges posed by local optima during helical reconstruction of amyloids.
  • To introduce an open-source method for generating improved 3D initial models for amyloid structure determination.

Main Methods:

  • Discussion of helical reconstruction principles relevant to amyloid structures.
  • Illustration of local optima issues and detection strategies in refinement.
  • Introduction of a novel method for calculating 3D initial models from reference-free 2D class averages.

Main Results:

  • The new method provides starting models closer to the global optimum, facilitating easier amyloid structure determination.
  • All presented methods are open-source and integrated into RELION-3.1.
  • The approach is demonstrated using a public dataset of tau filaments from Alzheimer's disease brains.

Conclusions:

  • The developed methods simplify the process of atomic-level amyloid structure determination using cryo-EM.
  • Improved initial models significantly reduce the difficulty associated with local optima in refinement.
  • The open-source nature of these tools promotes wider accessibility and application in structural biology research.