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Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules.
Authors:S A Darst   M Ahlers   P H Meller   E W Kubalek   R Blankenburg   H O Ribi   H Ringsdorf     R D Kornberg
Affiliation:Department of Cell Biology, Stanford University School of Medicine, California 94305.
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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