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Related Concept Videos

Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
Electron Tomography
Electron tomography can be performed either in TEM or STEM (scanning transmission...
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...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

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Related Experiment Video

Updated: May 10, 2026

Modeling Ligands into Maps Derived from Electron Cryomicroscopy
09:30

Modeling Ligands into Maps Derived from Electron Cryomicroscopy

Published on: July 19, 2024

Computational methods for constructing protein structure models from 3D electron microscopy maps.

Juan Esquivel-Rodríguez1, Daisuke Kihara

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

Journal of Structural Biology
|June 26, 2013
PubMed
Summary
This summary is machine-generated.

Cryo-electron microscopy (EM) now achieves high-resolution protein structure determination. This review covers computational methods for modeling 3D protein structures from EM density maps, including de novo and fitting approaches.

Keywords:
3D Zernike descriptor3DZDCATHClass, Architecture, Topology, Homologous superfamily. Acronym for the CATH protein structure databaseComputational algorithmDENDeformable Elastic NetworkEMEMDBENMElastic Network ModelElectron Microscopy Data BankElectron density mapElectron microscopyMCMDMDFFMacromolecular structure modelingMonte CarloNMANMFFNMRNormal Mode Flexible FittingNuclear Magnetic ResonancePDBProtein Data BankRMSDRoot Mean Square DeviationSVMStructure fittingelectron microscopymolecular dynamicsmolecular dynamics flexible fittingnormal mode analysissupport vector machine

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Single Particle Cryo-Electron Microscopy: From Sample to Structure
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Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

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Last Updated: May 10, 2026

Modeling Ligands into Maps Derived from Electron Cryomicroscopy
09:30

Modeling Ligands into Maps Derived from Electron Cryomicroscopy

Published on: July 19, 2024

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

Area of Science:

  • Structural Biology
  • Biophysics
  • Computational Biology

Background:

  • Cryo-electron microscopy (EM) has advanced significantly, enabling high-resolution protein structure determination.
  • Recent cryo-EM structures are solved at resolutions approaching 3Å, showcasing technological progress.
  • Interpreting cryo-EM data relies heavily on computational methods.

Purpose of the Study:

  • To review computational methods for modeling protein 3D structures from 3D cryo-EM density maps.
  • To categorize these methods into de novo and structure fitting approaches.
  • To provide a list of available computational tools for structure modeling.

Main Methods:

  • Focus on computational procedures for interpreting 3D EM density maps.
  • Discussion includes de novo methods for identifying structural elements within EM maps.
  • Coverage extends to structure fitting methods for incorporating known structures into low-resolution EM maps.

Main Results:

  • A comprehensive overview of computational strategies for protein structure modeling from cryo-EM data.
  • Categorization of methods based on their approach to interpreting EM density maps.
  • Identification and listing of relevant computational tools.

Conclusions:

  • Computational methods are crucial for advancing protein structure determination using cryo-EM.
  • A range of de novo and fitting methods are available for modeling structures.
  • The review provides valuable resources for researchers in the field.