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JAEA Reports

Risk communication activity which used "YUME Chisoukan" in the Horonobe Underground Research Center; FY2014

Fujiwara, Toshiyuki; Katada, Inao; Hoshino, Masato; Tokunaga, Hiroaki*; Horikoshi, Hidehiko*

JAEA-Review 2015-035, 103 Pages, 2016/03


Horonobe Underground Research Center managed by Japan Atomic Energy Agency (JAEA) is the Japan's best environment to understand the project of geological disposal of high-level radioactive waste of Japan because there is an underground research laboratory (URL) in the center besides an exhibition facility which explains the content of research conducted in the URL. In the area of the center, there is also an exhibition facility for the full-scale model of engineered barrier system of geological disposal. JAEA takes advantage of this opportunity to conduct public hearing including questionnaire research regarding the questions, anxieties and comments by the visitors for geological disposal project. This report summarizes the result of statistical analysis of 2457 comments by the visitors from April to November in 2014.

JAEA Reports

Risk communication activity which used "YUME Chisoukan" in the Horonobe Underground Research Center

Abe, Shinya; Katada, Inao; Hoshino, Masato; Tokunaga, Hiroaki*; Horikoshi, Hidehiko*

JAEA-Review 2014-034, 81 Pages, 2014/11


The Horonobe Underground Research Center conducts research and development to enhance the reliability of geological disposal technology, indicate the margin of technical safety for legally decided depth of repository, improve understanding of the deep geological environment, and promote greater public understanding for geological disposal technology. "YUME chisoukan" ceased its role as an exhibition facility as of end August 2012 as part of an administrative reform under the then Democratic Party rule, and came to be focused on disclosing the underground drifts to ascertain that JAEA is true to its tripartite agreement signed between the Hokkaido Prefecture, Town of Horonobe and JAEA (i.e., no nuclear materials will be used, etc.). It is also used as the facility to provide information on the research results of the Center. This report presents the statistical results of a questionnaire (2,566 responses) conducted from April to October 2013.

Journal Articles

"Crystal lattice engineering", an approach to engineer protein crystal contacts by creating intermolecular symmetry; Crystallization and structure determination of a mutant human RNase 1 with a hydrophobic interface of leucines

Yamada, Hidenori*; Tamada, Taro; Kosaka, Megumi*; Miyata, Kohei*; Fujiki, Shinya*; Tano, Masaru*; Moriya, Masayuki*; Yamanishi, Mamoru*; Honjo, Eijiro; Tada, Horiko*; et al.

Protein Science, 16(7), p.1389 - 1397, 2007/07

 Times Cited Count:39 Percentile:60.31(Biochemistry & Molecular Biology)

In an attempt to control protein incorporation in a crystal lattice, a leucine zipper-like hydrophobic interface (comprising four leucine residues) was introduced into a helical region (helix 2) of the human pancreatic ribonuclease 1 (RNase 1) that was predicted to form a suitable crystallization interface. Although crystallization of wild type RNase 1 has not yet been reported, the RNase 1 mutant having four leucines (4L-RNase 1) was successfully crystallized under several different conditions. The crystal structures were subsequently determined by X-ray crystallography by molecular replacement using the structure of bovine RNase A. The overall structure of 4L-RNase 1 is quite similar to that of the bovine RNase A, and the introduced leucine residues formed the designed crystal interface. To further characterize the role of the introduced leucine residues in crystallization of RNase 1, the number of leucines was reduced to three or two (3L- and 2L-RNase 1, respectively). Both mutants crystallized and a similar hydrophobic interface as in 4L-RNase 1 was observed. A related approach to engineer crystal contacts at helix 3 of RNase 1 (N4L-RNase 1) was also evaluated. N4L-RNase 1 also successfully crystallized, and formed the expected hydrophobic packing interface. These results suggest that appropriate introduction of a leucine zipper-like hydrophobic interface can promote intra molecular symmetry for more efficient protein crystallization in crystal lattice engineering efforts.

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