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Related Experiment Videos

The bacteriophage phi29 head-tail connector imaged at high resolution with the atomic force microscope in buffer

D J Müller1, A Engel, J L Carrascosa

  • 1M.E. Müller-Institute for Microscopic Structural Biology, Biozentrum, University of Basel, Switzerland.

The EMBO Journal
|May 15, 1997
PubMed
Summary

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Atomic force microscopy revealed the phi29 connector

Area of Science:

  • Structural biology
  • Biophysics

Background:

  • The phi29 connector is a viral portal protein essential for DNA packaging.
  • Previous studies have provided limited structural information on the phi29 connector.

Purpose of the Study:

  • To elucidate the detailed structure and flexibility of the phi29 connector using atomic force microscopy (AFM).
  • To complement existing structural data and provide insights into the connector's role in DNA packing.

Main Methods:

  • Imaging of two- and three-dimensional phi29 connector crystals in buffer solution using atomic force microscopy (AFM).
  • Analysis of crystal topographies to determine unit cell dimensions and symmetry.
  • High-resolution imaging to resolve connector subunits and channel dimensions.
  • Complementary analysis with three-dimensional reconstruction from electron microscopy data.

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Main Results:

  • phi29 connector crystals exhibit a rectangular unit cell (16.5 nm x 16.5 nm) with p42(1)2 symmetry.
  • Connector height is approximately 7.6 nm, with 12 resolved subunits showing right-handed vorticity.
  • A tronco-conical channel with varying diameters (3.7 nm wide domain, 1.7 nm narrow domain) was observed.
  • The narrow connector end demonstrated flexibility, extending at low forces and compressing at higher forces.

Conclusions:

  • AFM provides high-resolution structural details of the phi29 connector, consistent with previous findings.
  • The observed flexibility of the narrow connector end may play a role in DNA translocation or interaction.
  • Combined AFM and electron microscopy data offer new insights into the phi29 connector's function in DNA packaging.