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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

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...

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Related Experiment Video

Updated: May 14, 2026

Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope
09:49

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Consensus among multiple approaches as a reliability measure for flexible fitting into cryo-EM data.

Aqeel Ahmed1, Florence Tama

  • 1Department of Chemistry and Biochemistry, The University of Arizona, 1041 E. Lowell Street, Tucson, AZ 85721, USA. ahmedaq@umich.edu

Journal of Structural Biology
|February 19, 2013
PubMed
Summary

Consensus flexible fitting using multiple approaches improves the interpretation of cryo-electron microscopy (cryo-EM) data. Root-mean-square fluctuation (RMSF) among models serves as a local reliability measure for cryo-EM structure fitting.

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Last Updated: May 14, 2026

Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope
09:49

Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope

Published on: March 16, 2022

Cryo-EM and Single-Particle Analysis with Scipion
09:06

Cryo-EM and Single-Particle Analysis with Scipion

Published on: May 29, 2021

A Robust Single-Particle Cryo-Electron Microscopy (cryo-EM) Processing Workflow with cryoSPARC, RELION, and Scipion
13:43

A Robust Single-Particle Cryo-Electron Microscopy (cryo-EM) Processing Workflow with cryoSPARC, RELION, and Scipion

Published on: January 31, 2022

Area of Science:

  • Structural Biology
  • Biophysics
  • Computational Biology

Background:

  • Cryo-electron microscopy (cryo-EM) yields low-resolution density maps of large macromolecular assemblies.
  • Increasing deposition of high-resolution structures fitted into cryo-EM maps necessitates improved fitting protocols and reliability measures.

Purpose of the Study:

  • To validate a "consensus" flexible fitting approach using multiple methods for interpreting cryo-EM data.
  • To derive and assess a local reliability measure for assessing the accuracy of fitted models in cryo-EM density maps.

Main Methods:

  • Applied four different automated flexible fitting approaches to fit an initial structure into simulated cryo-EM density maps.
  • Compared conformations of models generated by different methods against a known target structure.
  • Calculated root-mean-square fluctuation (RMSF) profiles to assess per-residue reliability.

Main Results:

  • Models from different flexible fitting approaches often showed consensus in conformation and proximity to the target structure.
  • Non-consensus models were generally further from the target structure.
  • High correlation between RMSF profiles relative to average and target structures indicated consensus reflects accuracy at a per-residue level.

Conclusions:

  • The "consensus" flexible fitting approach enhances the interpretation of cryo-EM data.
  • Root-mean-square fluctuation (RMSF) among fitted models is a reliable measure for assessing local fit quality in cryo-EM.
  • Recommends community adoption of consensus flexible fitting and RMSF reporting for improved cryo-EM model reliability.