Prospects for X-ray Crystal Structure Analysis of Selenoproteins with SPring-8 Synchrotron Radiation
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概要
- 論文の詳細を見る
The impact of synchrotron radiation as a new X-ray source with its polychromatic nature and associated high intensity and fine collimation has brought important advances in the field of macromolecular crystallography. It has extended structure determinations of proteins to higher resolution, allowed use of smaller crystals with larger unit cells. In particular, selenoprotein is a suitable material for X-ray crystal structure analysis with synchrotron radiation, since its polychromatic nature and anomalous diffraction from the selenium atom(s) in the protein allow the multiple-wavelength anomalous-diffraction (MAD) method to be used for phase determination. RIKEN beam line I (BL45XU), installed in the SPring-8 synchrotron radiation facility, has been designed and developed to optimize MAD data collection based on a 'trichromatic concept'. This concept facilitates simultaneous data collection by use of a'trichromator', of three intensity data-sets at three different wavelengths from a single protein crystal, and thus results in the minimization of systematic errors in the measurement of anomalous diffraction by the MAD method. The X-ray crystallographic analysis of selenoprotein with SPring-8 synchrotron radiation, therefore, results in very fast data collection and high resolution structural analysis using a single protein crystal, which should lead to elucidation of the structure-function relationship of selenoprotein.
- 公益社団法人日本薬学会の論文
- 2000-12-01
著者
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YAMAMOTO Masaki
RIKEN Harima Institute
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Yamashita Eiki
Institute for Protein Research, Osaka University
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Meguro H
Tohoku Fukushi University
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Meguro H
Department Of Applied Biological Chemistry Faculty Of Agriculture Tohoku University
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Sato M
Graduate School Of Integrated Science Yokohama City University
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Misono H
Kochi Univ. Kochi Jpn
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Misono Haruo
Department Of Bioresources Science Faculty Of Agriculture Kochi University
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Misono Haruo
Department Of Bioresource Science Kochi University
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Misono Haruo
Laboratory Of Applied Microbiology Department Of Agricultural Chemistry Kochi University
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Sakurai Masahiro
Department Of Life Science Faculty Of Biocscience And Bioctechnology Tokyo Institute Of Technology
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Ueki T
Japan Synchrotron Radiation Research Institute (jasri)
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SATO Mamoru
Graduate School of Integrated Science, Yokohama City University
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Ueki Tatzuo
Japan Synchrotron Radiation Research Institute (jasri)
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Yamashita Eiki
Institute For Protein Research Osaka University
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Meguro Hiroshi
Kansei-fukushi Research Center Tohoku Fukushi University
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Kumasaka T
Riken Harima Inst. Hyogo
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Yamamoto Masaki
The Institute of Physical and Chemical Research (RIKEN)
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Kumasaka Takashi
The Institute of Physical and Chemical Research (RIKEN)
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Moriyama Hideaki
Japan Synchrotron Radiation Research Institute (JASRI)
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Yamamoto Masaki
Graduate School Of Natural Science And Technology Okayama University
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Kumasaka Takashi
Dep. Of Life Sci. Tokyo Inst. Of Technol.
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Sato Mamoru
Graduate School Of Integrated Science Yokohama City University
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Moriyama H
Department Of Life Science Faculty Of Biocscience And Bioctechnology Tokyo Institute Of Technology
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Yamashita Masao
Graduate School Of Natural Science And Technology Okayama University
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