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Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Advancing High-Resolution Imaging of Virus Assemblies in Liquid and Ice
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Advancing High-Resolution Imaging of Virus Assemblies in Liquid and Ice

Published on: July 20, 2022

Cystovirus maturation at atomic resolution.

David Veesler1, John E Johnson

  • 1Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Structure (London, England : 1993)
|August 13, 2013
PubMed
Summary
This summary is machine-generated.

Crystal structures of bacteriophage capsid proteins reveal striking similarities between Φ8 and Φ6, despite lacking sequence similarity. These findings offer new insights into viral mechanisms and evolution.

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Sample Preparation for Single Virion Atomic Force Microscopy and Super-resolution Fluorescence Imaging
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Related Experiment Videos

Last Updated: May 9, 2026

Advancing High-Resolution Imaging of Virus Assemblies in Liquid and Ice
08:31

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Published on: July 20, 2022

Correlative Light Electron Microscopy (CLEM) for Tracking and Imaging Viral Protein Associated Structures in Cryo-immobilized Cells
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Sample Preparation for Single Virion Atomic Force Microscopy and Super-resolution Fluorescence Imaging
05:31

Sample Preparation for Single Virion Atomic Force Microscopy and Super-resolution Fluorescence Imaging

Published on: January 2, 2014

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Cystoviruses are double-stranded RNA (dsRNA) viruses that infect bacteria.
  • Bacteriophages Φ8 and Φ6 are examples of cystoviruses.
  • Capsid protein P1 pentamers form the procapsid cores of these bacteriophages.

Purpose of the Study:

  • To determine the crystal structures of capsid protein P1 pentamers from bacteriophages Φ8 and Φ6.
  • To compare the structures and identify similarities and differences.
  • To gain mechanistic and evolutionary insights into cystoviruses.

Main Methods:

  • X-ray crystallography was used to determine the three-dimensional structures of the P1 pentamers.
  • Structural comparison and analysis were performed to assess similarities.

Main Results:

  • The crystal structures of P1 pentamers from Φ8 and Φ6 were determined.
  • The two structures exhibit a striking resemblance.
  • This resemblance is observed despite a lack of significant sequence similarity between the proteins.

Conclusions:

  • The conserved structural features of P1 pentamers suggest a common underlying mechanism for procapsid formation in cystoviruses.
  • The structural similarity provides insights into the evolutionary relationships between Φ8 and Φ6.
  • These findings contribute to a deeper understanding of bacteriophage assembly and evolution.