FEI Company Japan Ltd.

Tokyo, Japan

FEI Company Japan Ltd.

Tokyo, Japan
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PubMed | Tohoku University, FEI Company Japan Ltd., Kyushu University, Virginia Polytechnic Institute and State University and Mel Build Corporation
Type: Journal Article | Journal: Microscopy (Oxford, England) | Year: 2015

We have developed a newly designed straining specimen holder for in situ transmission electron microscopy (TEM) compatible with high-angle single tilt-axis electron tomography. The holder can deform a TEM specimen under tensile stress with the strain rate between 1.5 10(-6) and 5.2 10(-3) s(-1). We have also confirmed that the maximum tilt angle of the specimen holder reaches 60 with a rectangular shape aluminum specimen. The new specimen holder, termed as straining and tomography holder, will have wide range potential applications in materials science.


Yoshida K.,Japan Fine Ceramics Center | Yoshida K.,University of York | Yoshida K.,EcoTopia Science Institute | Bright A.,FEI Company Japan Ltd | And 3 more authors.
Journal of Electron Microscopy | Year: 2012

We study in situ behavior of platinum single atoms on amorphous carbon (a-carbon) using a spherical aberration-corrected transmission electron microscope (AC-TEM). Diffusion of single atoms, bi-atoms, clusters (<1 nm) and nanoparticles (<3 nm) was recorded in the same image with a time resolution of 1 s, and such diffusion matches the expected mechanism of Ostwald ripening, which was seen on these samples. In situ AC-TEM shows promise for dynamical observation of single atom diffusion, which is important for understanding nanosized catalysts and ceramic sintering processes. We apply in situ AC-TEM to image platinum (Pt) nanoparticles on a-carbon, which is a model catalyst system for the real Pt electrode catalysts using alloys and core-shell structures supported on carbon/oxide composite materials in the proton exchange membrane fuel cell. © The Author 2012. Published by Oxford University Press [on behalf of Japanese Society of Microscopy]. All rights reserved.


Bright A.N.,FEI Company Japan Ltd. | Yoshida K.,Nagoya University | Yoshida K.,Japan Fine Ceramics Center | Tanaka N.,Japan Fine Ceramics Center | Tanaka N.,EcoTopia Science Institute
Ultramicroscopy | Year: 2013

Environmental transmission electron microscopy (ETEM) enables the study of catalytic and other reaction processes as they occur with Angstrom-level resolution. The microscope used is a dedicated ETEM (Titan ETEM, FEI Company) with a differential pumping vacuum system and apertures, allowing aberration corrected high-resolution transmission electron microscopy (HRTEM) imaging to be performed with gas pressures up to 20. mbar in the sample area and with significant advantages over membrane-type E-cell holders. The effect on image resolution of varying the nitrogen gas pressure, electron beam current density and total beam current were measured using information limit (Young's fringes) on a standard cross grating sample and from silicon crystal lattice imaging. As expected, increasing gas pressure causes a decrease in HRTEM image resolution. However, the total electron beam current also causes big changes in the image resolution (lower beam current giving better resolution), whereas varying the beam current density has almost no effect on resolution, a result that has not been reported previously. This behavior is seen even with zero-loss filtered imaging, which we believe shows that the drop in resolution is caused by elastic scattering at gas ions created by the incident electron beam. Suitable conditions for acquiring high resolution images in a gas environment are discussed. Lattice images at nitrogen pressures up to 16. mbar are shown, with 0.12. nm information transfer at 4. mbar. © 2012 Elsevier B.V.


Ohta K.,Kurume University | Sadayama S.,Fukuoka University | Sadayama S.,FEI Company Japan Ltd. | Togo A.,Kurume University | And 3 more authors.
Micron | Year: 2012

The beam deceleration (BD) method for scanning electron microscopes (SEM) also referred to as "retarding" was applied to back-scattered electron (BSE) imaging of the flat block face of a resin embedded biological specimen under low accelerating voltage and low beam current conditions. BSE imaging was performed with 0-4. kV of BD on en bloc stained rat hepatocyte. BD drastically enhanced the compositional contrast of the specimen and also improved the resolution at low landing energy levels (1.5-3. keV) and a low beam current (10. pA). These effects also functioned in long working distance observation, however, stage tilting caused uncorrectable astigmatism in BD observation. Stage tilting is mechanically required for a FIB/SEM, so we designed a novel specimen holder to minimize the unfavorable tilting effect. The FIB/SEM 3D reconstruction using the new holder showed a reasonable contrast and resolution high enough to analyze individual cell organelles and also the mitochondrial cristae structures (∼5. nm) of the hepatocyte. These results indicate the advantages of BD for block face imaging of biological materials such as cells and tissues under low-voltage and low beam current conditions. © 2011 Elsevier Ltd.


Yoshida K.,Nagoya University | Yoshida K.,Japan Fine Ceramics Center | Xudong Z.,EcoTopia Science Institute | Bright A.N.,FEI Company Japan Ltd | And 3 more authors.
Nanotechnology | Year: 2013

Spherical-aberration-corrected environmental transmission electron microscopy (AC-ETEM) was applied to study the catalytic activity of platinum/amorphous carbon electrode catalysts in proton-exchange-membrane fuel cells (PEMFCs). These electrode catalysts were characterized in different atmospheres, such as hydrogen and air, and a conventional high vacuum of 10 -5 Pa. A high-speed charge coupled device camera was used to capture real-time movies to dynamically study the diffusion and reconstruction of nanoparticles with an information transfer down to 0.1 nm, a time resolution below 0.2 s and an acceleration voltage of 300 kV. With such high spatial and time resolution, AC-ETEM permits the visualization of surface-atom behaviour that dominates the coalescence and surface-reconstruction processes of the nanoparticles. To contribute to the development of robust PEMFC platinum/amorphous carbon electrode catalysts, the change in the specific surface area of platinum particles was evaluated in hydrogen and air atmospheres. The deactivation of such catalysts during cycle operation is a serious problem that must be resolved for the practical use of PEMFCs in real vehicles. In this paper, the mechanism for the deactivation of platinum/amorphous carbon electrode catalysts is discussed using the decay rate of the specific surface area of platinum particles, measured first in a vacuum and then in hydrogen and air atmospheres for comparison. © 2013 IOP Publishing Ltd.


PubMed | Institute of Physiological science, Juntendo University, FEI Company Japan Ltd. and Kurume University
Type: | Journal: Scientific reports | Year: 2015

Block-face imaging is a scanning electron microscopic technique which enables easier acquisition of serial ultrastructural images directly from the surface of resin-embedded biological samples with a similar quality to transmission electron micrographs. In the present study, we analyzed the three-dimensional architecture of podocytes using serial block-face imaging. It was previously believed that podocytes are divided into three kinds of subcellular compartment: cell body, primary process, and foot process, which are simply aligned in this order. When the reconstructed podocytes were viewed from their basal side, the foot processes were branched from a ridge-like prominence, which was formed on the basal surface of the primary process and was similar to the usual foot processes in structure. Moreover, from the cell body, the foot processes were also emerged via the ridge-like prominence, as found in the primary process. The ridge-like prominence anchored the cell body and primary process to the glomerular basement membrane, and connected the foot processes to the cell body and primary process. In conclusion, serial block-face imaging is a powerful tool for clear understanding the three-dimensional architecture of podocytes through its ability to reveal novel structures which were difficult to determine by conventional transmission and scanning electron microscopes alone.


Aramaki S.,Kyushu Institute of Technology | Mayanagi K.,Kyushu University | Jin M.,Osaka City University | Aoyama K.,FEI Company Japan Ltd | And 2 more authors.
Cytoskeleton | Year: 2016

Filopodia are finger-like protrusions at the leading edge of migrating cells that play a crucial antennal function during cell motility. It is known that actin filaments are bundled hexagonally and provide rigidity to filopodia by virtue of fascin, which plays a central role in actin filament bundling. However, the molecular mechanisms underlying their formation remain unclear. Here, we observed the filopodia of intact whole cells fixed by rapid freezing and revealed their three-dimensional structure by cryo-electron tomography and image processing; the actin filament bundling structure by fascin was clarified at high resolution under physiological conditions. It was found that actin filaments in vivo were more numerous than in bundles reconstructed in vitro, and each filopodial actin filament had limited variability in helical twisting. In addition, statistical analysis of actin filament bundles unveiled their detailed architecture. In filopodia, actin filaments had highly ordered structures, and the shift between cross-links of each adjacent actin filament was approximately 2.7 nm, similar to the monomer repeat of actin filaments. We then proposed a plausible actin-fascin cross-link model at the amino acid level and identified three fascin binding sites on two adjacent actin filaments: one filament bound fascin at two discrete, widely separated regions and the other bound fascin in a single small region. We propose that these two different binding modalities should confer rigid bundles that retain flexibility and dynamic performance. © 2016 Wiley Periodicals, Inc. © 2016 Wiley Periodicals, Inc.


PubMed | Kyushu Institute of Technology, FEI Company Japan Ltd, Osaka City University and Kyushu University
Type: Journal Article | Journal: Cytoskeleton (Hoboken, N.J.) | Year: 2016

Filopodia are finger-like protrusions at the leading edge of migrating cells that play a crucial antennal function during cell motility. It is known that actin filaments are bundled hexagonally and provide rigidity to filopodia by virtue of fascin, which plays a central role in actin filament bundling. However, the molecular mechanisms underlying their formation remain unclear. Here, we observed the filopodia of intact whole cells fixed by rapid freezing and revealed their three-dimensional structure by cryo-electron tomography and image processing; the actin filament bundling structure by fascin was clarified at high resolution under physiological conditions. It was found that actin filaments in vivo were more numerous than in bundles reconstructed in vitro, and each filopodial actin filament had limited variability in helical twisting. In addition, statistical analysis of actin filament bundles unveiled their detailed architecture. In filopodia, actin filaments had highly ordered structures, and the shift between cross-links of each adjacent actin filament was approximately 2.7 nm, similar to the monomer repeat of actin filaments. We then proposed a plausible actin-fascin cross-link model at the amino acid level and identified three fascin binding sites on two adjacent actin filaments: one filament bound fascin at two discrete, widely separated regions and the other bound fascin in a single small region. We propose that these two different binding modalities should confer rigid bundles that retain flexibility and dynamic performance. 2016 Wiley Periodicals, Inc.


Noda T.,Tokyo Medical University | Sugita Y.,Tokyo Medical University | Aoyama K.,FEI Company Japan Ltd. | Aoyama K.,Osaka University | And 10 more authors.
Nature Communications | Year: 2012

The influenza A virus genome consists of eight single-stranded negative-sense RNA (vRNA) segments. Although genome segmentation provides advantages such as genetic reassortment, which contributes to the emergence of novel strains with pandemic potential, it complicates the genome packaging of progeny virions. Here we elucidate, using electron tomography, the three-dimensional structure of ribonucleoprotein complexes (RNPs) within progeny virions. Each virion is packed with eight well-organized RNPs that possess rod-like structures of different lengths. Multiple interactions are found among the RNPs. The position of the eight RNPs is not consistent among virions, but a pattern suggests the existence of a specific mechanism for assembly of these RNPs. Analyses of budding progeny virions suggest two independent roles for the viral spike proteins: RNP association on the plasma membrane and the subsequent formation of the virion shell. Our data provide further insights into the mechanisms responsible for segmented-genome packaging into virions. © 2012 Macmillan Publishers Limited. All rights reserved.


Hata S.,Kyushu University | Miyazaki H.,Mel Build | Miyazaki S.,FEI Company Japan Ltd. | Mitsuhara M.,Kyushu University | And 9 more authors.
Ultramicroscopy | Year: 2011

Electron tomography requires a wide angular range of specimen-tilt for a reliable three-dimensional (3D) reconstruction. Although specimen holders are commercially available for tomography, they have several limitations, including tilting capability in only one or two axes at most, e.g. tilt-rotate. For amorphous specimens, the image contrast depends on mass and thickness only and the single-tilt holder is adequate for most tomographic image acquisitions. On the other hand, for crystalline materials where image contrast is strongly dependent on diffraction conditions, current commercially available tomography holders are inadequate, because they lack tilt capability in all three orthogonal axes needed to maintain a constant diffraction condition over the whole tilt range. We have developed a high-angle triple-axis (HATA) tomography specimen holder capable of high-angle tilting for the primary horizontal axis with tilting capability in the other (orthogonal) horizontal and vertical axes. This allows the user to trim the specimen tilt to obtain the desired diffraction condition over the whole tilt range of the tomography series. To demonstrate its capabilities, we have used this triple-axis tomography holder with a dual-axis tilt series (the specimen was rotated by 90° ex-situ between series) to obtain tomographic reconstructions of dislocation arrangements in plastically deformed austenitic steel foils. © 2011 Elsevier B.V.

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