An open source/real-time atomic force microscope architecture to perform customizable force spectroscopy experiments

Year: 2009

Authors: Materassi D., Baschieri P., Tiribilli B., Zuccheri G., Samori B.

Autors Affiliation: Department of Electrical and Computer Engineering, University of Minnesota, 200 Union St. SE, 55455Minneapolis, Minnesota, USA;
Institute for Chemical and Physical Processes, Consiglio Nazionale delle Ricerche, Via G. Moruzzi 1, I-56124 Pisa, Italy;
Istituto Sistemi Complessi, Consiglio Nazionale delle Ricerche, Via Madonna del Piano 10, I-50019 Sesto Fiorentino (FI), Italy;
Department of Biochemistry G. Moruzzi, S3 Center of the National Institute for the Physics of the Matter (CNR), Italian Interuniversity Consortium for Materials Science and Technology (INSTM), University of Bologna, Via Irnerio, 48, I-40126 Bologna, Italy

Abstract: We describe the realization of an atomic force microscope architecture. designed to perform customizable experiments in a flexible and automatic way. Novel technological contributions are given by the software implementation platform (RTAI-LINUX), which is free and open source, and from a functional point of view, by the implementation of hard real-time control algorithms. Some other technical solutions such as a new way to estimate the optical lever constant are described as well. The adoption of this architecture provides many degrees of freedom in the device behavior and, furthermore, allows one to obtain a flexible experimental instrument at a relatively low cost. In particular, we show how such a system has been employed to obtain measures in sophisticated single-molecule force spectroscopy experiments [Fernandez and Li, Science 303, 1674 (2004)]. Experimental results on proteins already studied using the same methodologies are provided in order to show the reliability of the measure system. (C) 2009 American Institute of Physics. [DOI: 10.1063/1.3194046]

Journal/Review: REVIEW OF SCIENTIFIC INSTRUMENTS

Volume: 80 (8)      Pages from: 84301  to: 84301

KeyWords: AFM; protein folding;
DOI: 10.1063/1.3194046

ImpactFactor: 1.521
Citations: 10
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