Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules. |
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Authors: | S A Darst M Ahlers P H Meller E W Kubalek R Blankenburg H O Ribi H Ringsdorf R D Kornberg |
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Affiliation: | Department of Cell Biology, Stanford University School of Medicine, California 94305. |
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Abstract: | Streptavidin forms two-dimensional crystals when specifically bound to layers of biotinylated lipids at the air/water interface. The three-dimensional structure of streptavidin determined from the crystals by electron crystallography corresponds well with the structure determined by x-ray crystallography. Comparison of the electron and x-ray crystallographic structures reveals the occurrence of free biotin-binding sites on the surface of the two-dimensional crystals facing the aqueous solution. The free biotin-binding sites could be specifically labeled with biotinylated ferritin. The streptavidin/biotinylated lipid system may provide a general approach for the formation of two-dimensional crystals of biotinylated macromolecules. |
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