AFM structural study of the molecular chaperone GroEL and its two-dimensional crystals: an ideal "living" calibration sample

Ultramicroscopy. 2002 Oct;93(1):83-9. doi: 10.1016/s0304-3991(02)00149-3.

Abstract

Supramolecular complexes, such as chaperonins, are suitable samples for atomic force microscope structural studies because they have a very well defined shape. High-resolution images can be made using tapping mode in liquid under native conditions. Details about the two-dimensional structures formed onto the surface upon adsorption and of the single protein can be observed. Dissection of the upper ring of the supramolecular complex as a result of the applied lateral force through scanning tip is observed. Finally, the combination of lateral convolution and tip penetration into the cavity of chaperonins offers a direct evaluation of the tip convolution effect on images of macromolecular samples.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calibration
  • Chaperonin 60 / chemistry*
  • Crystallization
  • Image Processing, Computer-Assisted
  • Microscopy, Atomic Force / instrumentation
  • Microscopy, Atomic Force / methods*
  • Molecular Chaperones / chemistry*
  • Protein Conformation

Substances

  • Chaperonin 60
  • Molecular Chaperones