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Related Experiment Videos

Crystallographic analysis of acrosomal bundle from Limulus sperm.

M F Schmid1, P Matsudaira, T W Jeng

  • 1Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030.

Journal of Molecular Biology
|September 20, 1991
PubMed
Summary

The structure of Limulus sperm acrosomal process bundles, made of actin and a 102 kDa protein, was revealed using advanced imaging. Crystallographic packing of twisted filaments likely controls bundle assembly and diameter.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Cell Biology

Background:

  • The acrosomal process in Limulus sperm is crucial for fertilization.
  • It contains a unique filament bundle composed of actin and a 102 kDa protein.
  • Understanding the structure of this bundle is key to deciphering its function.

Purpose of the Study:

  • To investigate the detailed structure of the Limulus sperm acrosomal process bundle.
  • To elucidate the relationship between filament arrangement and bundle stability.
  • To propose a model for bundle assembly control.

Main Methods:

  • Electron cryomicroscopy for high-resolution imaging.
  • X-ray scattering to analyze structural parameters.
  • Crystallographic image analysis to determine symmetry and unit cell dimensions.

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Main Results:

  • The bundle exhibits quasi-crystalline properties with P1 space group symmetry.
  • A unit cell reveals a helical repeat of filaments, consistent with actin.
  • A 24 Å projection map shows filaments with 21 screw symmetry, a non-crystallographic element.

Conclusions:

  • The structural analysis provides insights into the filament organization within the bundle.
  • Crystallographic packing of twisted filaments is proposed as the mechanism controlling bundle assembly and diameter.
  • This finding contributes to understanding the biophysical principles governing cytoskeletal structures.