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Imaging streptavidin 2D crystals on biotinylated lipid monolayers at high resolution with the atomic force microscope
Author(s) -
SCHEURING S.,
MÜLLER D. J.,
RINGLER P.,
HEYMANN J. B.,
ENGEL A.
Publication year - 1999
Publication title -
journal of microscopy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.569
H-Index - 111
eISSN - 1365-2818
pISSN - 0022-2720
DOI - 10.1046/j.1365-2818.1999.00434.x
Subject(s) - streptavidin , monolayer , biotinylation , highly oriented pyrolytic graphite , materials science , resolution (logic) , crystallography , tetramer , chemistry , nanotechnology , analytical chemistry (journal) , biotin , scanning tunneling microscope , chromatography , organic chemistry , biochemistry , artificial intelligence , computer science , enzyme
Streptavidin crystals were grown on biotinylated lipid monolayers at an air/water interface and transferred onto highly oriented pyrolytic graphite (HOPG). These arrays could be imaged to a resolution below 1 nm using the atomic force microscope. The surface topographs obtained were compared with negative‐stain electron microscopy images and the atomic model as determined by X‐ray crystallography. The streptavidin tetramer (60 kDa) exposes two free biotin‐binding sites to the buffer solution, while two are occupied by linkage to the lipid monolayer. Therefore, the streptavidin 2D crystals can be used as nanoscale matrices for binding biotinylated compounds. Furthermore, this HOPG‐based preparation method provides a general novel approach to study the structure of protein arrays assembled on lipid monolayers with the AFM.