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Biophys J, August 1999, p. 1150-1158, Vol. 77, No. 2
*M. E. Müller Institute for Structural Biology, Biozentrum, CH-4056 Basel, Switzerland; #Forschungszentrum Jülich, IBI-2: Structural Biology, D-52425 Jülich, Germany; and §Digital Instruments, Santa Barbara, California 93117 USA
Compared to contact-mode atomic force microscopy (CMAFM),
tapping-mode atomic force microscopy (TMAFM) has the advantage of allowing imaging surfaces of macromolecules, even when they are only
weakly attached to the support. In this study, TMAFM is applied to two
different regular protein layers whose structures are known to great
detail, the purple membrane from Halobacterium salinarum and the hexagonally packed intermediate (HPI) layer from
Deinococcus radiodurans, to assess the faithfulness of
high-resolution TMAFM images. Topographs exhibited a lateral resolution
between 1.1 and 1.5 nm and a vertical resolution of ~0.1 nm. For all
protein surfaces, TMAFM and CMAFM topographs were in excellent
agreement. TMAFM was capable of imaging the fragile polypeptide loop
connecting the transmembrane 
-helices E and F of bacteriorhodopsin
in its native extended conformation. The standard deviation (SD) of
averages calculated from TMAFM topographs exhibited an enhanced minimum (between 0.1 and 0.9 nm) that can be assigned to the higher noise of
the raw data. However, the SD difference, indicating the flexibility of
protein subunits, exhibited an excellent agreement between the two
imaging modes. This demonstrates that the recently invented imaging-mode TMAFM has the ability to faithfully record high-resolution images and has sufficient sensitivity to contour individual peptide loops without detectable deformations.
Biophys J, August 1999, p. 1150-1158, Vol. 77, No. 2
© 1999 by the Biophysical Society 0006-3495/99/08/1150/09 $2.00
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