Ultralow emittance beam production based on Doppler laser cooling and coupling resonance

Noda, Akira*; Nakao, Masao*; Okamoto, Hiromi*; Osaki, Kazuya*; Yuri, Yosuke; Soda, Hikaru*; Tongu, Hiromu*; Jimbo, Koichi*; Grieser, M.*; He, Z.*; et al.

Proceedings of 5th International Particle Accelerator Conference (IPAC '14) (Internet), p.28 - 33, 2014/07

http://accelconf.web.cern.ch/AccelConf/IPAC2014/papers/moza01.pdf

Simulation study on transverse laser cooling and crystallization of heavy-ion beams at the cooler storage ring S-LSR

Yuri, Yosuke; Osaki, Kazuya*; Okamoto, Hiromi*; He, Z.*; Soda, Hikaru*; Noda, Akira*; Nakao, Masao*; Tongu, Hiromu*; Jimbo, Koichi*

Proceedings of Workshop on Beam Cooling and Related Topics (COOL '13) (Internet), p.162 - 165, 2013/11

http://accelconf.web.cern.ch/AccelConf/COOL2013/papers/tham1ha03.pdf

Parameter optimization for multi-dimensional laser cooling of an ion beam in the storage ring S-LSR

He, Z.*; Wei, J.*; Osaki, Kazuya*; Okamoto, Hiromi*; Noda, Akira*; Nakao, Masao*; Soda, Hikaru*; Yuri, Yosuke; Jimbo, Koichi*

Proceedings of 25th North American Particle Accelerator Conference (NA-PAC '13) (Internet), p.1298 - 1300, 2013/09

http://accelconf.web.cern.ch/AccelConf/PAC2013/papers/thpho01.pdf

Approach to the low temperature state oriented for crystalline beam

Noda, Akira*; Nakao, Masao*; Soda, Hikaru*; Tongu, Hiromu*; Jimbo, Koichi*; Okamoto, Hiromi*; Osaki, Kazuya*; Yuri, Yosuke; Meshkov, I.*; Smirnov, A.*; et al.

Proceedings of 23rd Russian Particle Accelerator Conference (RuPAC 2012) (Internet), p.48 - 52, 2012/09

http://accelconf.web.cern.ch/AccelConf/rupac2012/papers/tuxch03.pdf

Controlled beam scraping oriented for efficient indirect transverse laser cooling

Noda, Akira*; Nakao, Masao*; Soda, Hikaru*; Tongu, Hiromu*; Jimbo, Koichi*; Okamoto, Hiromi*; Osaki, Kazuya*; Yuri, Yosuke; Grieser, M.*; He, Z.*

Proceedings of 9th Annual Meeting of Particle Accelerator Society of Japan (Internet), p.72 - 74, 2012/08

http://www.pasj.jp/web_publish/pasj9/proceedings/PDF/WELR/WELR03.pdf

Challenge for more efficient transverse laser cooling for beam crystallization

Noda, Akira*; Nakao, Masao*; Soda, Hikaru*; Tongu, Hiromu*; Ito, Kiyokazu*; Okamoto, Hiromi*; Osaki, Kazuya*; Yuri, Yosuke; Jimbo, Koichi*; Grieser, M.*; et al.

Proceedings of 3rd International Particle Accelerator Conference (IPAC '12) (Internet), p.394 - 396, 2012/05

http://accelconf.web.cern.ch/accelconf/IPAC2012/papers/moppd012.pdf

Extension of the Newcomb equation into the vacuum for the stability analysis of tokamak edge plasmas

Aiba, Nobuyuki; Tokuda, Shinji; Ishizawa, Tomoko*; Okamoto, Masao*

Computer Physics Communications, 175(4), p.269 - 289, 2006/08

https://doi.org/10.1016/j.cpc.2006.04.008

The formulation for solving numerically the two-dimensional Newcomb equation has been extended to calculate the vacuum energy integral by using a vector potential method. According to this extention, a stability code MARG2D has been adapted, and coded for parallel computing in order to reduce substantially the CPU time. The MARG2D code enables a fast stability analysis of ideal external MHD modes from low to high toroidal mode numbers on the basis of the single physical model, and then the code works as a powerful tool in an integrated simulation where it is combined with transport codes, and also in the analysis of tokamak edge plasma experiments.

Crystallization of a 2:2 complex of Granulocyte-Colony Stimulating Factor (GCSF) with the ligand-binding region of the GCSF receptor

Honjo, Eijiro; Tamada, Taro; Maeda, Yoshitake*; Koshiba, Takumi*; Matsukura, Yasuko*; Okamoto, Tomoyuki*; Ishibashi, Matsujiro*; Tokunaga, Masao*; Kuroki, Ryota

Acta Crystallographica Section F, 61(8), p.788 - 790, 2005/08

https://doi.org/10.1107/S1744309105023080

Granulocyte colony-stimulating factor (GCSF) receptor receives signals for regulating the proliferation and differentiation of the precursor cells of granulocytes. The complex composed of two GCSFs and two GCSF receptors was crystallized. The crystal of the complex was grown in 1.0 M sodium formate and 0.1 M sodium acetate (pH4.6). It belongs to the space group 422 (or its enantiomorph 422) with unit cell dimensions of = = 110.1 , = 331.8 . However, the diffraction data from the crystal beyond 5 resolution could not be collected. Since the heterogeneity of GCSF receptor seems to interrupt growth of good quality crystals, the GCSF receptor was fractionated by achromatography. Crystals of GCSF/fractionated GCSF receptor complex were grown as a new crystal form in 0.2 M ammonium phosphate. The new crystal diffracts beyond 3.0 resolution and belongs to space group 321 (or its enantiomorph 321) with unit-cell parameters = = 134.8, = 105.7 .

Simulation studies of high energy particles and neo-classical transport

Okamoto, Masao*; Hamamatsu, Kiyotaka; Murakami, Sadayoshi*; Nakajima, Noriyoshi*

Purazuma, Kaku Yugo Gakkai-Shi, 77(6), p.536 - 546, 2001/06

https://ci.nii.ac.jp/naid/110003825635

no abstracts in English

Homodimeric crossover structure of the human GCSF-receptor signaling complex

Tamada, Taro; Honjo, Eijiro; Maeda, Yoshitake*; Okamoto, Tomoyuki*; Ishibashi, Matsujiro*; Tokunaga, Masao*; Kuroki, Ryota

no journal, , 

We have succeeded in crystallization of 2:2 complex between human granulocyte colony-stimulating factor (hGCSF) and the Ig-like and CRH domains of human GCSF-R (hGCSF-R) and determined its tertiary structure by X-ray crystallography at 2.8 resolution. The signaling 2:2 complex is formed via cross-over interactions between the Ig-like domain of hGCSF-R and the neighboring hGCSF, forming a two-fold axis of crystallographic symmetry. This conformation is quite different from that of the heterogeneous mGCSF-R complex, and more closely resembles the 2:2:2 active assembly of human interleukin-6 (IL-6), human IL-6 -receptor and human gp130 (which is a shared signal transducing receptor for several cytokines), and the 2:2 assembly of viral IL-6 and human gp130. The Ig-like domain cross-over structure necessary for GCSF-R activation is consistent with previously reported thermodynamic and mutational analyses.