Structural information, resolution, and noise in high-resolution atomic force microscopy topographs.

ABSTRACT: AFM has developed into a powerful tool in structural biology, providing topographs of proteins under close-to-native conditions and featuring an outstanding signal/noise ratio. However, the imaging mechanism exhibits particularities: fast and slow scan axis represent two independent image acquisition axes. Additionally, unknown tip geometry and tip-sample interaction render the contrast transfer function nondefinable. Hence, the interpretation of AFM topographs remained difficult. How can noise and distortions present in AFM images be quantified? How does the number of molecule topographs merged influence the structural information provided by averages? What is the resolution of topographs? Here, we find that in high-resolution AFM topographs, many molecule images are only slightly disturb

SUBMITTER: Fechner P 

PROVIDER: S-EPMC2711429 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature