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Research

Research

BDR researchers coming from diverse research fields are working together to achieve higher goals.

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BDR hosts annual symposium and regular seminars inviting international scientists in life science.

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Careers & Study

BDR embraces people from diverse backgrounds, and strives to create an open and supportive setting for research.

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BDR communicates the appeal and significance of our research to society through the use of various media and activities.

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About Us

About Us

Exploring the scientific foundations of life through interdisciplinary approaches to address society’s problems.

Photo of Team leder, Atsuko Iwane

Team Leader
Atsuko Iwane Ph.D.

Laboratory for Cell Field Structure

Location Hiroshima

E-mailatsuko.iwane[at]riken.jp

Please replace [at] with @.

Electron microscopy (EM) offers the best in resolution of extremely small biological specimens, providing images of the minutest of organelles and molecules that are responsible for phenomena fundamental to life including cell division, differentiation and proliferation. The resulting fine structural information has been extraordinary in helping our understanding of how morphology and function relate.  We seek to image several target molecules and organelles, including the mitochondria and chloroplasts, and their surrounding environments inside a cell by using two different electron microscopy technologies. The first is Cryo-EM tomography, which produces a 3D image by scanning the field of view at multiple angles over an angular range from -70 degrees to 70 degrees relative to the perpendicular of the specimen plane used in transmission electron microscopy (TEM). The second is focused ion beam scanning electron microscopy (FIB-SEM), which uses SEM to scan a number of sections that are created by FIB. In this aim, we will combine our electron microscopy system with fluorescence microscopy to conduct dual imaging of the specimen in the same field of view. This will provide information on the dynamics of the specimen, which will complement the structure information and give us better understanding of the relationship between cell fate and cell morphology.

Research Theme

  • Development of stainless cell imaging by Cryo-TEM
  • Whole cell structure reconstruction by three-dimensional FIB-SEM

Selected Publications

Mizuno K, Shiozawa K, Katoh TA, et al.
Role of Ca2+ transients at the node of the mouse embryo in breaking of left-right symmetry.
Science Advances 6, eaba1195 (2020) doi: 10.1126/sciadv.aba1195

Miyamoto T, Hosoba K, Itabashi T, et al.
Insufficiency of ciliary cholesterol in hereditary Zellweger syndrome.
The EMBO journal 39(12), e103499 (2020) doi: 10.15252/embj.2019103499

Fujii T, Iwane AH, Yanagida T, Namba K.
Direct visualization of secondary structures of F-actin by electron cryomicroscopy.
Nature 467(7316), 724-728 (2010) doi: 10.1038/nature09372

Nishikawa S, Arimoto I, Ikezaki K, et al.
Switch between Large Hand-Over-Hand and Small Inchworm-like Steps in Myosin VI.
Cell 142(6), 879-888 (2010) doi: 10.1016/j.cell.2010.08.033

Watanabe TM, Yanagida T, Iwane AH.
Single molecular observation of self-regulated kinesin motility.
Biochemistry 49, 4654-4661, (2010) doi: 10.1021/bi9021582

Iwane AH, Morimatsu M, Yanagida T.
Recombinant alpha-actin for specific fluorescent labeling.
Proceedings of the Japan Academy Series B-Physical and Biological Sciences 85(10), 491-499 (2009) doi: 10.2183/pjab.85.491

Iwaki M, Iwane AH, Shimokawa T, et al.
Brownian search-and-catch mechanism for myosin-VI steps.
Nature Chemical Biology 5(6), 403-405 (2009) doi: 10.1038/nchembio.171

Iwane AH. Tanaka H, Morimoto S, et al.
The neck domain of myosin II primarily regulates the actomyosin kinetics, not the 10.1016/j.jmb.2005.08.013stepsize.
Journal of Molecular Biology 353, 213-221, (2005) doi: 10.1016/j.jmb.2005.08.013

Tanaka H, Homma K, Iwane AH, et al.
The motor domain determines the large step of myosin-V.
Nature 415, 192-195, (2002) doi: 10.1038/415192a

Kitamura K, Tokunaga M, Iwane AH, Yanagida T.
A single myosin head moves along an actin filament with regular steps of 5.3 nanometres.
Nature 397, 129-134, (1999) doi: 10.1038/16403

Iwane AH, Funatsu T, Harada Y, et al.
Single molecular assay of the individual ATP turnovers by a myosin-GFP fusion protein expressed in vitro.
FEBS Letters 407, 235-238, (1997) doi: 10.1016/S0014-5793(97)00359-1

Iwane AH, Kitamura K, Tokunaga M, Yanagida T.
Myosin subfragment-1 is fully equipped with factors essential for motor function.
Biochemical and Biophysical Research Communications 230, 76-80, (1997) doi: 10.1006/bbrc.1996.5861

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