AFM structural study of the molecular chaperone GroEL and its two-dimensional crystals: an ideal "living" calibration sample.
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.
Valle
F
F
Institut de Physique de la Matière Condensèe, BSP, Université de Lausanne, Dorigny, Switzerland. francesco.valle@ipmc.unil.ch
DeRose
J A
JA
Dietler
G
G
Kawe
M
M
Plückthun
A
A
Semenza
G
G
D002138:Calibration; D018834:Chaperonin 60 / Q000737:chemistry*; D003460:Crystallization; D007091:Image Processing, Computer-Assisted; D018625:Microscopy, Atomic Force / Q000295:instrumentation / Q000379:methods*; D018832:Molecular Chaperones / Q000737:chemistry*; D011487:Protein Conformation
D018834:Chaperonin 60; D018832:Molecular Chaperones