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Nakazawa, Osamu; Takiya, Hiroaki; Murakami, Masashi; Donomae, Yasushi; Meguro, Yoshihiro
JAEA-Review 2023-012, 6 Pages, 2023/08
JAEA-Review-2023-012.pdf:0.93MB
The selection of back-end technology development issues to be prioritized and their schedule of the Japan Atomic Energy Agency (JAEA) have been put together as the "Strategic Roadmap for Back-end Technology Development." The results of questionnaires on development technologies (seeds) and technical issues (needs) within JAEA conducted in FY2022 were reflected in the selection. The issues were extracted from among those that match the seeds and needs, from the perspective of early implementation in the work front and the perspective of common issues, and nine themes were selected. We will build a cross-organizational implementation framework within JAEA and aim to implement the development results in the work front as well as social implementation.
Mizuhashi, Kiyoshi; Uno, Sadanori; Okoshi, Kiyonori; Chiba, Atsuya; Yamada, Keisuke; Saito, Yuichi; Ishii, Yasuyuki; Sato, Takahiro; Sakai, Takuro; Yokota, Wataru; et al.
JAEA-Review 2006-042, JAEA Takasaki Annual Report 2005, P. 197, 2007/02
Three electrostatic accelerators were almost operated smoothly for various experiments in FY 2005. The yearly operation time of each accelerator amounts to 1974, 2359.9, 1859.9 hour for the tandem, the single-ended and the ion implanter, respectively. Main trouble was a short circuit of a part of the ion source in the single-ended accelerator. This lets to the suspension of operation for fifteen days. As features in FY 2005, the generation of the power cut by thunderbolts and large earthquakes were abounding. By this natural force, the Turbo-molecular pump was broken, experiment was interrupted and then the inspection of accelerator facility was carried out every time. New beam acceleration and improvement of each accelerator were carried out.
Tanaka, Hirokazu; Koizumi, Satoshi; Hashimoto, Takeji; Kurosaki, Kazuhiro*; Omae, Masashi*; Kobayashi, Shiro*
Physica B; Condensed Matter, 385-386(1), p.814 - 817, 2006/11
Times Cited Count：3 Percentile：17.92(Physics, Condensed Matter)We have investigated a self-assembling process of cellulose artificially synthesized via enzymatic polymerization by means of in-situ and time-resolved small-angle neutron scattering (SANS). The results elucidated the following: (1) cellulose molecules were synthesized at a special reaction site of the enzyme (cellulase) located on or near the smooth surface of the self-assembled enzymes formed in the reaction medium; (2) the synthesized molecules associated themselves via diffusion-limited aggregation (DLA) and crystallized into fibrils and (3) the fibrils formed the aggregates, which had the surface fractal dimension D
increasing from 2 to 2.3 with the reaction time, on the smooth surface of the enzyme aggregates.
Hashimoto, Takeji; Tanaka, Hirokazu; Koizumi, Satoshi; Kurosaki, Kazuhiro*; Omae, Masashi*; Kobayashi, Shiro*
Biomacromolecules, 7(9), p.2479 - 2482, 2006/09
Times Cited Count：13 Percentile：38.26(Biochemistry & Molecular Biology)no abstracts in English
Mizuhashi, Kiyoshi; Uno, Sadanori; Okoshi, Kiyonori; Chiba, Atsuya; Yamada, Keisuke; Saito, Yuichi; Ishii, Yasuyuki; Sakai, Takuro; Sato, Takahiro; Yokota, Wataru; et al.
JAEA-Review 2005-001, TIARA Annual Report 2004, P. 371, 2006/01
no abstracts in English
Hashimoto, Takeji; Tanaka, Hirokazu; Koizumi, Satoshi; Kurosaki, Kazuhiro*; Omae, Masashi*; Kobayashi, Shiro*
no journal, ,
We have investigated self-assembling process of cellulose artificially synthesized via enzymatic polymerization by means of in-situ and time-resolved SANS (Small-angle Neutron Scattering). The results elucidated the followings: (1) Cellulose molecules synthesized at a special reaction site of the enzyme (cellulase) located on or near the smooth surface of self-assembled enzymes formed in the reaction medium; (2) The synthesized molecules associated themselves via DLA (diffusion-limited association) and crystallized into fibrils; (3) The fibrils formed the aggregates, which had surface fractal dimension Ds increasing from 2 to 2.3 with the reaction time, on the smooth surface of the enzyme aggregates.
Mizuhashi, Kiyoshi; Uno, Sadanori; Okoshi, Kiyonori; Chiba, Atsuya; Yamada, Keisuke; Saito, Yuichi; Ishii, Yasuyuki; Sato, Takahiro; Yokota, Wataru; Kitano, Toshihiko*; et al.
no journal, ,
no abstracts in English
Mizuhashi, Kiyoshi; Uno, Sadanori; Okoshi, Kiyonori; Chiba, Atsuya; Yamada, Keisuke; Saito, Yuichi; Ishii, Yasuyuki; Sato, Takahiro; Sakai, Takuro; Yokota, Wataru; et al.
no journal, ,
no abstracts in English
