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Acta Cryst. (2014). A70, C1299
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A century ago, crystallogtaphy ushered in the era of modern science & technology in Japan. The beginning of modern crystallography in Japan dates back to 1913. Torahiko Terada (Tokyo Imperial University) demonstrated X-ray diffraction[1] and Shoji Nishikawa (Tokyo Imperial University) reported on X-ray patterns of fibrous, lamellar and granular substances[2]. In 1936, Ukichiro Nakaya (Hokkaido University) successfully classified natural snow crystals and made the first artificial snow crystals. In the last half-century, developments in crystallography helped form thriving manufacturing sectors such as the semiconductor industry, the iron and steel industries, the pharmaceutical industry, the electronics industry, the textile industry, and the polymer industry, as well as a wide array of academic research.

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Acta Cryst. (2014). A70, C1304
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"We can find many seeds of crystallography in Japanese culture. Most of the family crests have symmetry elements such as rotation axes and mirror symmetry elements. Sekka-zue, a picture book of 86 kinds of crystals of snow, was made by Toshitura Doi, who is a feudal lord in Edo-period and he observed snow using a microscope in nineteenth century. In recent years, people enjoy to make crystal structures, polyhedrons, carbon nanotube, quasicrystal etc. by origami, the art of folding paper [1]. In the field of science, the Japanese crystallography has contributed to explore culture and art. An excellent example is unveiling the original color of Japanese painting "Red and White Plum Blossoms" by Korin Ogata [2]. Prof. Izumi Nakai (Tokyo University of Science) developed an X-ray fluorescence analyzer and an X-ray powder diffractometer designated to the investigation of cultural and art works and had succeeded in reproducing the silver-colored waves through computer graphics after X-ray analyses of crystals on the painting. The scientific approach by Prof. Nakai et al. unveiled the mystery of cultural heritage of ancient near east, ancient Egypt etc. and is being to contribute to insight into the history of human culture. [1] An event to enjoy making crystals by origami is under contemplation. [2] The symposium ""Crystallography which revives heritages"" was held on February 16, 2014 at Atami in Japan."

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Acta Cryst. (2014). A70, C1309
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Divers Japanese Science and Technology has advanced together with the progress of crystallography in biology, chemistry, physics, materials science, metallurgy, electronics, engineering, geoscience, etc. Based on the highly scientific and crystallographic technology, Japan has been a great contributor in developing of high-end X-ray generator, electron microscope as well as large scale Photon Science facilities, such as Photon Factory (SR), SPring-8 (SR), J-PARC (Neutron) and SACLA (XFEL). Under such background, we promote IYCr2014 with the partnership of 36 academic societies in the field of pure and applied sciences. In the last half-century, developments in crystallography have also helped thriving manufacturing sectors such as the semiconductor, the iron and steel, the pharmaceuticals, the electronics, the textile, and the chemical industries. Some of the recent impressive outcomes in Japan are fundamental findings of photosynthesis [1] and pristine asteroid [2]. Crystallography in Japan keeps promoting our nationwide projects grappling with global problems such as environment and food, and will contribute to realize a sustainable society.

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Acta Cryst. (2014). A70, C1501
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The voltage-gated proton channel, Hv1 (VSOP) has a voltage-sensor domain (VSD) but lacks an authentic pore domain, and the VSD of Hv1 plays dual roles of voltage sensing and proton permeation. Hv1 is required for high-level superoxide production by phagocytes through its tight functional coupling with NADPH oxidase to eliminate pathogens. Hv1 is also expressed in human sperm and has been suggested to regulate motility through activating pH-sensitive calcium channels. The activities of Hv1 also have pathological implications, such as exacerbation of ischemic brain damage and progression of cancer. In this study, our crystal structure of mouse Hv1 (mHv1) showed a "closed umbrella" shape with a long helix consisting of the cytoplasmic coiled-coil and the voltage-sensing helix, S4, and featured a wide inner-accessible vestibule. We also found a Zn2+ ion at the extracellular region of mHv1 protomer. The binding of Zn2+ strongly suggested that the crystal structure of mHv1 represents the resting state, since Zn2+ specifically inhibits activities of voltage-gated proton channels. Actually, two out of three arginines as sensor residues (R204 and R207) were located lower than the conserved phenylalanine, F146, on the S2 in a charge transfer center. This makes contrast with previous structures of other VSDs in the activated state where many positive residues of S4 were located upper than the conserved phenylalanine. Additionally, the crystal structure of mHv1 highlighted two hydrophobic barriers. Aspartic acid (D108), which is critical for proton selective permeation, was located facing intracellular vestibule below the inner hydrophobic barrier, thereby being accessible to water from the cytoplasm. Another hydrophobic layer of extracellular side probably ensures interruption of the proton pathway of mHv1 in resting state. These findings provide a novel platform for understanding the general principles of voltage sensing and proton permeation.

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Acta Cryst. (2014). A70, C1684
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Biological macromolecular assemblies play significant roles in many biological reaction systems, including energy transfer, protein synthesis, protein degradation and signal transduction. A detailed understanding of the functions of the macromolecular assemblies requires information derived from three-dimensional atomic structures. X-ray crystal structure analysis is one of the most powerful methods to determine the three-dimensional structures of macromolecular assemblies at atomic level. Since features of crystals of biological macromolecular assemblies are extremely weak diffraction power and narrow space between the diffraction spots, it is essential to use high brilliance and high paralleled synchrotron radiation for diffraction data collection from crystals of biological macromolecular assemblies. The Institute for Protein Research (IPR) of Osaka University is operating a beamline for crystal structure analysis of biological macromolecular assemblies at SPring-8 (BL44XU). This beamline is designed to collect high quality diffraction data from biological macromolecular assembly crystals with large unit cells. The light source of this beamline is a SPring-8 standard type in-vacuum undulator. Liquid nitrogen cooled double crystal monochromator and horizontal focusing mirror are used as the optical components. BSS (Beamline Scheduling Software), which is SPring-8 protein crystallography beamline standard GUI, is installed to unify user operation throughout protein crystallography beamlines in the SPring-8. We have recently upgraded to a high speed air-bearing goniostat and installed a high performance CCD detector, MX-300HE. Present status and future plan of the beamline will be presented.
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