Journal article
AFM structural study of the molecular chaperone GroEL and its two-dimensional crystals: an ideal "living" calibration sample.
- Valle F Institut de Physique de la Matière Condensèe, BSP, Université de Lausanne, Dorigny, Switzerland. francesco.valle@ipmc.unil.ch
- DeRose JA
- Dietler G
- Kawe M
- Plückthun A
- Semenza G
- 2002-10-17
Published in:
- Ultramicroscopy. - 2002
Calibration
Chaperonin 60
Crystallization
Image Processing, Computer-Assisted
Microscopy, Atomic Force
Molecular Chaperones
Protein Conformation
English
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.
- Language
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- English
- Open access status
- closed
- Identifiers
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- DOI 10.1016/s0304-3991(02)00149-3
- PMID 12380652
- Persistent URL
- https://sonar.ch/global/documents/139168
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