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High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE
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Published on: May 16, 2017

Problems in fitting high resolution structures into electron microscopic reconstructions.

Edward H Egelman1

  • 1Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia 22908-0733.

HFSP Journal
|May 14, 2009
PubMed
Summary
This summary is machine-generated.

Electron microscopy (EM) can determine protein structures. Docking high-resolution component structures into lower-resolution EM reconstructions builds pseudoatomic models, but limitations can cause ambiguities, especially with homology models.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Biochemistry

Background:

  • Recent advances in electron microscopy (EM) enable near-atomic resolution imaging of protein complexes.
  • However, many protein assemblies and polymers exhibit internal disorder, limiting EM resolution.
  • High-resolution structures of individual components (from X-ray crystallography or NMR) are often available.

Purpose of the Study:

  • To review the strengths and limitations of using EM to build pseudoatomic models of protein quaternary structure.
  • To highlight challenges in docking component structures into lower-resolution EM reconstructions, particularly for protein polymers.
  • To discuss ambiguities arising from resolution limitations and the problematic use of homology models.

Main Methods:

  • Integration of high-resolution component structures (e.g., from crystallography, NMR) into lower-resolution EM reconstructions.
  • Computational modeling to build pseudoatomic models of protein complex quaternary structure.
  • Analysis of resolution limitations and their impact on model building accuracy.

Main Results:

  • EM is powerful for building pseudoatomic models of protein assemblies by docking known component structures.
  • Resolution limits in EM reconstructions can introduce ambiguities in model building, which may not be resolvable with existing data.
  • The use of homology models for quaternary structure is particularly problematic due to conserved tertiary but divergent quaternary structures.

Conclusions:

  • Docking high-resolution structures into EM reconstructions is a valuable strategy for understanding protein quaternary structure.
  • Careful consideration of EM resolution limitations is crucial to avoid model ambiguities.
  • Caution is advised when using homology models for quaternary structure due to potential divergence.