膜融合を利用したバクテリオロドプシンの結晶化法 A 3D Crystal of Bacteriorhodopsin Obtained by Successive Fusion of the Vesicular Assemblies

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Bacteriorhodopsin, the sole protein in the purple membrane of <I>Halobacterium salinarium</I>, functions as a light-driven proton pump. To obtain it's three-dimensional crystal, we have developed a new crystallization method which does not involve any step of complete destruction of the membrane. First, purple membrane was incubated at high temperature with neutral detergent and ammonium sulfate so that the membrane was converted into uniformly sized spherical vesicles. Then the vesicles were condensed at low temperature, where fusion of the vesicles produced a hexagonal crystal which is made up of planar membranes. Structural analysis showed that the trimeric structure of bacteriorhodopsin was retained in the crystal. The native lipid bound to a specific site in the protein was suggested to play an important role in maintaining the higher-order structure of the membrane.

収録刊行物

  • 日本結晶学会誌  

    日本結晶学会誌 42(2), 171-175, 2000-04-30 

    The Crystallographic Society of Japan

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各種コード

  • NII論文ID(NAID)
    10004673426
  • 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
    5335123
  • 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  NDL  J-STAGE 
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