低温蛋白質結晶構造解析 Cryogenic Protein Crystallography

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Cryogenic protein crystallography is now the indispensable method in structural biology. In this method, protein crystals are rapidly cooled by low temperature nitrogen gas or liquid ethane, and diffraction intensity data are collected at cryogenic temperature. By applying this method, the X-radiation damage of protein crystals are drastically decreased, and we can easily obtain diffraction data even for highly radiation-sensitive protein crystals. This method has been applied to investigate the hydration structures around protein molecules and to analyze the structure of reaction-intermediates of proteins. Here, we briefly report the procedures and the experimental techniques using the newly developed devices and discuss the advantages and the disadvantages of this method. In addition, we describe the application of this method to crystallographically investigate the mechanism of the glassy transition observed in the vibrational states of protein molecules around 200 K.

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  • 日本結晶学会誌  

    日本結晶学会誌 41(1), 57-65, 1999-02-28 

    The Crystallographic Society of Japan

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各種コード

  • NII論文ID(NAID)
    10002591445
  • NII書誌ID(NCID)
    AN00188364
  • 本文言語コード
    JPN
  • 資料種別
    ART
  • ISSN
    03694585
  • NDL 記事登録ID
    4672586
  • NDL 雑誌分類
    ZM46(科学技術--地球科学--岩石・鉱物・鉱床)
  • NDL 請求記号
    Z15-138
  • データ提供元
    CJP書誌  CJP引用  NDL  J-STAGE 
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