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Related Experiment Videos

Refinement of herpesvirus B-capsid structure on parallel supercomputers

Z H Zhou1, W Chiu, K Haskell

  • 1Texas Center for Advanced Molecular Computation, University of Houston, 77204-3476, USA.

Biophysical Journal
|February 4, 1998
PubMed
Summary

Researchers used electron cryomicroscopy to determine the 3D structure of the herpesvirus B-capsid. This advanced technique achieved 13-Å resolution, revealing new details about its protein subunits.

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Area of Science:

  • Structural biology
  • Virology
  • Computational biology

Background:

  • Determining the high-resolution three-dimensional structure of viruses is crucial for understanding their assembly and function.
  • Herpesvirus B-capsid, a large icosahedral particle, presents significant computational challenges for structural determination.

Purpose of the Study:

  • To obtain the high-resolution three-dimensional structure of the herpesvirus B-capsid using electron cryomicroscopy.
  • To describe and evaluate the use of shared-memory multiprocessor computers for computationally intensive global refinement in icosahedral reconstruction.

Main Methods:

  • Utilized electron cryomicroscopy and icosahedral reconstruction techniques.
  • Employed common-lines-based local and global refinement procedures for particle determination and orientation.

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  • Implemented and evaluated a parallel refinement program on shared-memory supercomputers for global refinement.

    • Main Results:

    • Achieved a 13-Å resolution three-dimensional structure of the herpesvirus B-capsid from 355-particle images.
    • Demonstrated the efficiency and speedup of parallel processing for global refinement on supercomputers.
    • The resulting structural map revealed novel features and interactions of protein subunits (penton, hexon, triplex).

    Conclusions:

    • The study successfully determined the detailed structure of the herpesvirus B-capsid.
    • Shared-memory multiprocessor computers are effective for accelerating computationally demanding steps in cryo-EM reconstruction.
    • The high-resolution map provides new insights into the molecular architecture of this T=16 icosahedral virus.