Two-dimensional crystallization of streptavidin by nonspecific binding to a surface film: study with a scanning electron microscope

T. Furuno, H. Sasabe

研究成果: Article査読

24 被引用数 (Scopus)

抄録

A two-dimensional (2D) crystal of streptavidin has been obtained by a nonspecific binding method. The protein molecules were bound and formed a dense packing on the film of poly(1-benzyl-L-histidine) spread at the surface of protein solution. The surface film was moderately heated to stimulate crystallization of bound streptavidin. A potential of this method for obtaining 2D crystals of soluble proteins is demonstrated. The present 2D crystal structure of streptavidin resembles that previously obtained by specific binding to biotinylated lipid. We show in addition that the 2D array of protein with usual size approximately 50 A can be imaged using a high resolution scanning electron microscope (HR-SEM) and subject to structural analysis at low resolution. Various limitations in HR-SEM degrade considerably the image quality. However, the usability of a bulk plate as specimen support would make HR-SEM a convenient tool, when such a substrate must be considered in application of protein arrays, and if an intrinsic low resolution is acceptable.

本文言語English
ページ(範囲)1714-1717
ページ数4
ジャーナルBiophysical Journal
65
4
DOI
出版ステータスPublished - 1993
外部発表はい

ASJC Scopus subject areas

  • 生物理学

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