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Esser, S. P.*; Rahlff, J.*; Zhao, W.*; Predl, M.*; Plewka, J.*; Sures, K.*; Wimmer, F.*; Lee, J.*; Adam, P. S.*; McGonigle, J.*; et al.
Nature Microbiology (Internet), 8(9), p.1619 - 1633, 2023/09
Times Cited Count：7 Percentile：81.27(Microbiology)
archaeaSchoelmerich, M. C.*; Oubouter, H. T.*; Sachdeva, R.*; Penev, P. I.*; Amano, Yuki; West-Roberts, J.*; Welte, C. U.*; Banfield, J. F.*
Nature Communications (Internet), 13, p.7085_1 - 7085_11, 2022/11
Times Cited Count：12 Percentile：73.20(Multidisciplinary Sciences)Fukuda, Kenji; Watanabe, Yusuke; Murakami, Hiroaki; Amano, Yuki; Aosai, Daisuke*; Hara, Naohiro*
JAEA-Data/Code 2020-012, 80 Pages, 2020/10
JAEA-Data-Code-2020-012.pdf:3.55MB
Japan Atomic Energy Agency has been investigating groundwater chemistry to understand the influence of excavation and maintenance of underground facilities as part of the Mizunami Underground Research Laboratory (MIU) Project in Mizunami, Gifu, Japan. In this report, we compiled data of groundwater chemistry and microbiology obtained at the MIU in the fiscal year 2019. In terms of ensuring traceability of data, basic information (e.g. sampling location, sampling time, sampling method and analytical method) and methodology for quality control are described.
Endo, Kiyoshi*; Shibata, Yasushi*; Yoshida, Fumiyo*; Nakai, Kei*; Yamamoto, Tetsuya*; Matsumura, Akira*; Ishii, Keizo*; Sakai, Takuro; Sato, Takahiro; Oikawa, Masakazu*; et al.
Proceedings of 11th World Congress on Neutron Capture Therapy (ISNCT-11) (CD-ROM), 2 Pages, 2004/10
Micro PIXE, which is installed in a single end accelerator in JAERI, was used for quantitative analysis of boron and gadolinium distribution in a cell level. The micro beam of 1 
m diameter is possible to observe the distribution. In the adjustment procedure of the sample, first is a fix of mylar film by using a glass ring and a bite ring of 2cm diameter. Next the 9L cells were scattered on the washed film, and is cultivated on 37
C in medium until they form the mono-layer. After the Gd-BOPTA was added, it incubates for the 24-72 hour on 37C. The film is washed in the THAM liquid, and is directly put on liquid nitrogen. A vacuum drying for 24 hours is conducted in order to fix a film on holder. It is important to uniformly fix the cell in distribution analysis in the cell using Micro PIXE. In recent result, it became possible that the distribution of P, S, Gd, etc. was analyzed. But we could not distinguish whether K and Gd exist in the cell or whether it exists around the cell. It was indicated that these elements was leaked by the reason of cell breaking or other on the cytoplasm.
resolutionChatake, Toshiyuki*; Kurihara, Kazuo; Tanaka, Ichiro*; Tsyba, I.*; Bau, R.*; Jenney, F. E. Jr.*; Adams, M. W. W.*; Niimura, Nobuo
Acta Crystallographica Section D, 60(8), p.1364 - 1373, 2004/08
Times Cited Count：34 Percentile：88.59(Biochemical Research Methods)A neutron diffraction study has been carried out at 1.6 resolution on a mutant rubredoxin from 
using the BIX-3 single-crystal diffractometer at the JRR-3 reactor of JAERI. In order to study the unusual thermostability of rubredoxin from 
, the hydrogen-bonding patterns were compared between the native and a 'triple-mutant' variant where three residues were changed so that they are identical to those in a mesophilic rubredoxin. In the present study, some minor changes were found between the wild-type and mutant proteins in the hydrogen-bonding patterns of the Trp3/Tyr3 region. The H/D-exchange ratios in the protein were also studied. The results suggest that the backbone amide bonds near the four Cys residues of the FeS
redox center are most resistant to H/D exchange. In addition, the 1.6 resolution of the present neutron structure determination has revealed a more detailed picture than previously available of some portions of the water structure, including ordered and disordered O-D bonds.
by BIX-3, a single-crystal diffractometer for biomacromoleculesKurihara, Kazuo; Tanaka, Ichiro*; Chatake, Toshiyuki*; Adams, M. W. W.*; Jenney, F. E. Jr.*; Moiseeva, N.*; Bau, R.*; Niimura, Nobuo
Proceedings of the National Academy of Sciences of the United States of America, 101(31), p.11215 - 11220, 2004/08
Times Cited Count：48 Percentile：60.27(Multidisciplinary Sciences)The structure of a rubredoxin (Rd) from , an organism that grows optimally at 100 C, was determined using the neutron single-crystal diffractometer for biological macromolecules (BIX-3) at the JRR-3 reactor of JAERI. Data were collected at room temperature up to a resolution of 1.5 , and the completeness of the data set was 81.9 %. The model contains 306 H atoms and 50 D atoms. A total of 37 hydration water molecules were identified. The model has been refined to final agreement factors of 
= 18.6 % and 
= 21.7 %. Several orientations of the O-D bonds of side chains, whose assignments from X-ray data were previously ambiguous, were clearly visible in the neutron structure. While most backbone N-H bonds had undergone some degree of H/D exchange throughout the molecule, five H atom positions still had distinctly negative (H) peaks. The neutron Fourier maps clearly showed the details of an extensive set of H bonds involving the ND
terminus that may contribute to the unusual thermostability of this molecule.
Kurihara, Kazuo; Tanaka, Ichiro*; Niimura, Nobuo
Nihon Kessho Gakkai-Shi, 46(3), p.193 - 200, 2004/05
Neutron diffraction provides an experimental method of directly locating hydrogen atoms in proteins and nucleic acids, and the development of the neutron imaging plate (NIP) became a breakthrough event in neutron protein crystallography. A high-resolution neutron diffractometers dedicated to biological macromolecules (BIX-3, BIX-4) with the NIP have been constructed at Japan Atomic Energy Research Institute. The detailed structure of the diffractometer and the systematic procedure of the neutron diffraction experiment from the crystallization of a large single crystal to the data collection and the data processing, and the future prospect of the neutron diffractometry in proteins will be presented.
Niimura, Nobuo; Kurihara, Kazuo; Tanaka, Ichiro
Kagaku, 59(2), p.46 - 47, 2004/02
no abstracts in English
Kume, Tamikazu; Watanabe, Kazuo*; Tano, Shigemitsu*
JAERI-Conf 2002-001, 171 Pages, 2002/02
JAERI-Conf-2002-001.pdf:15.66MB
no abstracts in English
Kurihara, Kazuo; Tanaka, Ichiro; Adams, M. W. W.*; Jenney, F. E. Jr.*; Moiseeva, N.*; Bau, R.*; Niimura, Nobuo
Journal of the Physical Society of Japan, Vol.70, Supplement A, p.400 - 402, 2001/05
With the new single-crystal diffractometer BIX-3 at the JRR-3M reactor of JAERI, a single-crystal neutron diffraction analysis of the structure of the small protein rubredoxin from the hyperthermophile Pyrococcus furiosus is currently under way. Data were collected at room temperature up to a resolution of 1.5 
intervals in 
and exposure times ranging from 60 to 77 minutes per frame. The completeness factor of the 1.5-
. Included in the refinement are 301 hydrogen atoms and 40 deuterium atoms, and 29 water molecules were also identified. In the present model, the current value for R and R
are 24.0 
and 26.3 , respectively.
Sekine, Toshiaki
Program of Regional Training Workshop on GMP in Production of Tc99m Generator, 7 Pages, 1999/10
no abstracts in English
Konishi, Hiroyuki; Yokoya, Akinari; Shiwaku, Hideaki; Motohashi, Haruhiko; ; Kashihara, Yasuharu*; ; Harami, Taikan; Sasaki, Teikichi; Maeta, Hiroshi; et al.
Nuclear Instruments and Methods in Physics Research A, 372, p.322 - 332, 1996/00
Times Cited Count：72 Percentile：97.67(Instruments & Instrumentation)no abstracts in English
Sekine, Toshiaki
JAERI-Conf 95-017, 0, p.209 - 214, 1995/09
no abstracts in English
Funahashi, Satoru; Niimura, Nobuo*
JAERI-M 92-213, 95 Pages, 1993/01
no abstracts in English
