Using high-speed atomic force microscopy (high-speed AFM) and super-resolution in-liquid AFM, we are studying the structure and dynamics of biomolecules. Unlike conventional methods, high-speed AFM allows simultaneous recording of the structure and dynamics of functioning molecules at high spatiotemporal resolution, and hence, makes it possible to directly understanding how biomolecules operate. Super-resolution AFM can visualize even the secondary structures of proteins (alpha-helix and beta-sheet), and therefore, we can study the details of the structure-function relationship. The Imaging Research Division will be established in 2011 after recruiting three new members　

Ongoing Research: Using high-speed AFM, we are studying dynamic biomolecular processes to understand how biomolecules operate. Thus far, we have succeeded in imaging dynamic processes including walking myosin V along actin filaments and structural changes of bacteriorhodopsin in response to light illuminaion. We are further attempting to image the dynamic behaviour of  other molecules such as myosin VI, dynein, and various intrinsically disordered proteins. Using super-resolution AFM, we are studying water layer structures surrounding material surfaces and the secondary structure of proteins. When a new high-speed AFM instrument for cell imaging is established to some extent, we will also conduct AFM imaging of cells.

Selected Publications

T. Ando, "High-speed atomic force microscopy coming of age", Nanotechnology 23: 062001 (27 pp)  (2012).

K. Igarashi, T. Uchihashi, A. Koivula, M. Wada, S. Kimura, T. Okamoto, M. Penttilä, T. Ando, and M. Samejima, "Traffic jams reduce hydrolytic efficiency of cellulase on cellulose surface", Science 333:1279-1282 (2011).

T. Uchihashi, R. Iino, T. Ando, and H. Noji, "High-speed atomic force microscopy reveals rotory catalysis of rotorless F1-ATPase, Science 333: 755-758 (2011).

N. Kodera, D. Yamamoto, R. Ishikawa, and T. Ando, "Video imaging of walking myosin V by high-speed atomic force microscopy", Nature 468: 72-76 (2010). (supplementary movies) (supplementary info) (News & View)

M. Shibata, T. Uchihashi, H. Yamashita, H. Kandori, and T. Ando, "Structural changes in bacteriorhodopsin in response to alternate illumination observed by high-speed atomic force microscopy",  Angewande Chemie International edition 50: 4410 –4413 (2011).

P.-E. Milhiet, D. Yamamoto., O. Berthoumieu, P. Dosset, C. Le Grimellec, J.-M.Verdier, S. Marchal, and T. Ando, "Deciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy", PLos One 5 (11): e13240 (8 pp) (2010). (Movie S1, Movie S2, Movie S3) (supplementary info)

D. Yamamoto, T. Uchihashi, N. Kodera, H. Yamashita, S. Nishikori, T. Ogura, M. Shibata, and T. Ando, "High-speed atomic force microscopy techniques for observing dynamic biomolecular processes", Methods Enzymol. 475 (Part B): 541-564 (2010).

D. Yamamoto, T. Azuma, T. Uchihashi, H. Sasaki, H. Watanabe, T. Ando, and Y. Fukumori,  "Visualization and structural analysis of the bacterial magnetic organelle magnetosome using atomic force microscopy", Proc. Natl. Acad. Sci. USA 107: 9382-9387 (2010). (supplementary info) (supplementary movie)

S. Sugimoto, K. Yamanaka, S. Nishikori, A. Miyagi, T. Ando, and T. Ogura, "AAA+ chaperone ClpX regurates dynamics of prokaryotic cytoskeletal protein FtsZ", J. Biol. Chem. 285: 6648-6657 (2010).

M.-C. Giocondi, D. Yamamoto, E. Lesniewska, P.-E. Milhiet, T. Ando, and C. Le Grimellec, "Surface topography of membrane domains", Bioochim. Biophys. Acta.-Biomembranes 1798: 703-718 (2010)

M. Shibata, H. Yamashita, T. Uchihashi, H. Kandori, and T. Ando, "High-speed atomic force microscopy shows dynamic molecular processes in photo-activated bacteriorhodopsin", Nature Nanotechnology 5, 208 - 212 (2010).  (Supplementary Info) (Supplementary Movies) (npg asia materials highlight)

D. Yamamoto, N. Nagura, S. Omote, M. Taniguchi, and T. Ando, "Streptavidin 2D crystal substrates for visualizing biomolecular processes by atomic force microscopy", Biophys. J. 97(8): 2358–2367 (2009).

H. Yamashita, K. Voïtchovsky, T. Uchihashi, S. Antoranz Contera, J. F. Ryan, and T. Ando, "Dynamics of bacteriorhodopsin 2D crystal observed by high-speed atomic force microscopy", J. Struct. Biol. 167: 153-158 (2009).

http://www.sciencedirect.com/science/journal/10478477 (Supplementary Movie)

D. Yamamoto, T. Uchihashi, N. Kodera, and T. Ando, "Anisotropic diffusion of point defects in two-dimensional crystal of streptavidin observed by high-speed atomic force microscopy", Nanotechnol. 19: 384009 (9 pp) (2008). (Supplementary Movie)  

A. Miyagi, Y. Tsunaka, T. Uchihashi, K. Mayanagi, S. Hirose, K. Morikawa, and T. Ando, "Visualization of intrinsically disordered regions of proteins by high-speed atomic force microscopy", Chem. Phys. Chem. 9(13):1859-1866 (2008). (Supplementary Movies)

T. Ando, T. Uchihashi, N. Kodera, D. Yamamoto, M. Taniguchi, A. Miyagi, and H. Yamashita, "Invited Review: High-speed AFM and nano-visualization of biomolecular processes", Pflügers Archiv -Eur. J. Physiol. 456:211-225 (2008).

T. Ando, T. Uchihashi, N. Kodera, D. Yamamoto, M. Taniguchi, A. Miyagi, and H. Yamashita, "Review: High-speed atomic force microscopy for observing dynamic biomolecular processes", J. Mol. Recognit. 20:448-458 (2007).  

M. Yokokawa, C. Wada, T. Ando, N. Sakai , A. Yagi, S.H. Yoshimura, and K. Takeyasu, "Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL", EMBO J. 25:4567-4576 (2006). 

T. Ando, T. Uchihashi, N. Kodera, A. Miyagi, R. Nakakita, H. Yamashita, and M. Sakashita, "High-speed atomic force microscopy for studying the dynamic behavior of protein molecules at work", Jpn. J. Appl. Phys. 45(3B):1897-1903 (2006).

T. Ando, T. Uchihashi, N. Kodera, A. Miyagi, R. Nakakita, H. Yamashita, and K. Matada, "High-speed AFM for studying the dynamic behavior of protein molecules at work", Surf. Sci. Nanotechnol. 3:384-392 (2005)(Supplementary Data)

T. Ando, N. Kodera, Y. Naito, T. Kinoshita, K. Furuta, and Y.Y. Toyoshima, "A high-speed atomic force microscope for studying biological macromolecules in action", Chem. Phys. Chem. 4:1196-1202 (2003).

T. Ando, N. Kodera, E. Takai, D. Maruyama,  K. Saito, and A. Toda, "A High-speed atomic force microscope for studying biological macromolecules", Proc. Natl. Acad. Sci. USA  98:12468-12472 (2001).