Development of a High-Speed Laser-Free Atomic Force Microscopy

Author(s):  
Saeid Bashash ◽  
Reza Saeidpourazar ◽  
Nader Jalili

To reduce the cost and improve the speed of Atomic Force Microscopy (AFM) in molecular scale imaging of materials, we propose a laser-free AFM scheme augmented with an accurate control strategy for its scanning axes. It employs a piezoresistive sensing device with a high level of accuracy to avoid using the bulky and expensive laser interferometer. Change in the resistance of piezoelectric layer due to the deflection of microcantilever caused by the variation of surface topography is monitored through a Wheatstone bridge. Hence, it captures the surface topography without the use of laser and with nanometer scale accuracy. To improve the speed of imaging, however, a Lyapunov-based robust adaptive control strategy is implemented in the 2-DOF scanning stage. It has been demonstrated in an earlier publication that this control framework has superior performance over the conventional PID controllers typically used in commercial AFMs. The paper, then, demonstrates a set of experiments on a standard AFM calibration sample with 200 nm stepped topography. Results indicate accurate imaging of the sample up to the frequency of 30 Hz, for a 16μm×16μm scanning area, proving the feasibility of less costly and high speed AFM-based metrology.

2003 ◽  
Vol 15 (1) ◽  
pp. 108-114 ◽  
Author(s):  
G Schitter ◽  
F Allgöwer ◽  
A Stemmer

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Rina Hirano ◽  
Yasuhiro Arimura ◽  
Tomoya Kujirai ◽  
Mikihiro Shibata ◽  
Aya Okuda ◽  
...  

AbstractH2A.B is an evolutionarily distant histone H2A variant that accumulates on DNA repair sites, DNA replication sites, and actively transcribing regions in genomes. In cells, H2A.B exchanges rapidly in chromatin, but the mechanism has remained enigmatic. In the present study, we found that the H2A.B-H2B dimer incorporated within the nucleosome exchanges with the canonical H2A-H2B dimer without assistance from additional factors, such as histone chaperones and nucleosome remodelers. High-speed atomic force microscopy revealed that the H2A.B nucleosome, but not the canonical H2A nucleosome, transiently forms an intermediate “open conformation”, in which two H2A.B-H2B dimers may be detached from the H3-H4 tetramer and bind to the DNA regions near the entry/exit sites. Mutational analyses revealed that the H2A.B C-terminal region is responsible for the adoption of the open conformation and the H2A.B-H2B exchange in the nucleosome. These findings provide mechanistic insights into the histone exchange of the H2A.B nucleosome.


2006 ◽  
Vol 45 (3B) ◽  
pp. 1897-1903 ◽  
Author(s):  
Toshio Ando ◽  
Takayuki Uchihashi ◽  
Noriyuki Kodera ◽  
Atsushi Miyagi ◽  
Ryo Nakakita ◽  
...  

2011 ◽  
Vol 47 (17) ◽  
pp. 4974 ◽  
Author(s):  
Shigeto Inoue ◽  
Takayuki Uchihashi ◽  
Daisuke Yamamoto ◽  
Toshio Ando

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