Letter
Ultrastable Atomic Force Microscopy: Atomic-Scale Stability and Registration in Ambient Conditions
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JILA, National Institute of Standards and Technology and University of Colorado.
, ‡Department of Physics, University of Colorado.
, §Denver School of Science and Technology.
,
Department of Molecular, Cellular, and Developmental Biology, University of Colorado.
Abstract

Instrumental drift in atomic force microscopy (AFM) remains a critical, largely unaddressed issue that limits tip−sample stability, registration, and the signal-to-noise ratio during imaging. By scattering a laser off the apex of a commercial AFM tip, we locally measured and thereby actively controlled its three-dimensional position above a sample surface to <40 pm (Δf = 0.01−10 Hz) in air at room temperature. With this enhanced stability, we overcame the traditional need to scan rapidly while imaging and achieved a 5-fold increase in the image signal-to-noise ratio. Finally, we demonstrated atomic-scale (
100 pm) tip−sample stability and registration over tens of minutes with a series of AFM images on transparent substrates. The stabilization technique requires low laser power (<1 mW), imparts a minimal perturbation upon the cantilever, and is independent of the tip−sample interaction. This work extends atomic-scale tip−sample control, previously restricted to cryogenic temperatures and ultrahigh vacuum, to a wide range of perturbative operating environments.
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This article has been cited by 1 ACS Journal articles (1 most recent appear below).

Single-Molecule Force Spectroscopy from Nanodiscs: An Assay to Quantify Folding, Stability, and Interactions of Native Membrane Proteins
Michael Zocher, Christian Roos, Susanne Wegmann, Patrick D. Bosshart, Volker Dötsch, Frank Bernhard, and Daniel J. MüllerACS Nano2012 6 (1), 961-971Single-Molecule Force Spectroscopy from Nanodiscs: An Assay to Quantify Folding, Stability, and Interactions of Native Membrane Proteins
Michael Zocher, Christian Roos, Susanne Wegmann, Patrick D. Bosshart, Volker Dötsch, Frank Bernhard, and Daniel J. MüllerACS Nano2012 6 (1), 961-971Single-molecule force spectroscopy (SMFS) can quantify and localize inter- and intramolecular interactions that determine the folding, stability, and functional state of membrane proteins. To conduct SMFS the membranes embedding the membrane proteins must ...
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History
- Published In Issue April 08, 2009
- Article ASAPMarch 12, 2009
- Received: November 01, 2008
Revised: January 27, 2009
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