中国物理B ›› 2005, Vol. 14 ›› Issue (1): 1-5.doi: 10.1088/1009-1963/14/1/001

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Resolution improvement of electron micrographs by the direct method for biotin-binding protein streptavidin

李方华1, 王怀斌1, 古元新1, 范海福1, 阳世新2, 刘玉东3   

  1. (1)Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100080, China; (2)College of Life Science, Sichuan University, Chengdu 610064, China; (3)Lineberger Comprehensive Cancer Centre, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7295, USA
  • 收稿日期:2004-07-06 修回日期:2004-08-13 出版日期:2005-01-20 发布日期:2005-01-20
  • 基金资助:
    Natural Science Foundation of China (Grant Nos 19574073 and19634020)

Resolution improvement of electron micrographs by the direct method for biotin-binding protein streptavidin

Yang Shi-Xin (阳世新)a, Li Fang-Hua (李方华)b, Liu Yu-Dong (刘玉东)c, Wang Huai-Bin (王怀斌)b, Gu Yuan-Xin (古元新)b, Fan Hai-Fu (范海福)b   

  1. a College of Life Science, Sichuan University, Chengdu 610064, China; b Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100080, China; c Lineberger Comprehensive Cancer Centre, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7295, USA
  • Received:2004-07-06 Revised:2004-08-13 Online:2005-01-20 Published:2005-01-20
  • Supported by:
    Natural Science Foundation of China (Grant Nos 19574073 and19634020)

摘要: Direct-method phase extension has been applied to two-dimensional electrondiffraction data of the protein streptavidin. Structure-factor amplitudesfrom electron diffraction were combined with phases from the correspondingelectron micrographs. Maximum-entropy discrimination and cluster analysiswere used to derive a solution from a large number of random trials. The phase extension from 0.3 to 0.25nm led to substantial improvement of thereconstructed projection image quality.

关键词: electron crystallography, direct method, protein structure, streptavidin

Abstract: Direct-method phase extension has been applied to two-dimensional electrondiffraction data of the protein streptavidin. Structure-factor amplitudesfrom electron diffraction were combined with phases from the correspondingelectron micrographs. Maximum-entropy discrimination and cluster analysiswere used to derive a solution from a large number of random trials. The phase extension from 0.3 to 0.25nm led to substantial improvement of thereconstructed projection image quality.

Key words: electron crystallography, direct method, protein structure, streptavidin

中图分类号: 

  • 0290