Atomic force microscopy of a hydrated bacterial surface protein.
The protein surface layer of the bacterium Deinococcus radiodurans (HPI layer) was examined with an atomic force microscope (AFM). The measurements on the air-dried, but still hydrated layer were performed in the attractive imaging mode in which the forces between tip and sample are much smaller than in AFM in the repulsive mode or in scanning tunnelling microscopy (STM). The results are compared with STM and transmission electron microscopy (TEM) data.
Max-Planck Institut für Biochemie, Martinsried, Germany.
W
W
Wiegräbe
M
M
Nonnenmacher
R
R
Guckenberger
O
O
Wolter
D001426:Bacterial Proteins / Q000648:ultrastructure*; D006095:Gram-Positive Cocci / Q000648:ultrastructure*; D008565:Membrane Proteins / Q000648:ultrastructure*; D008854:Microscopy, Electron; D016252:Microscopy, Scanning Tunneling
D001426:Bacterial Proteins; D008565:Membrane Proteins