Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules.

Autor: Darst SA; Department of Cell Biology, Stanford University School of Medicine, California 94305., Ahlers M, Meller PH, Kubalek EW, Blankenburg R, Ribi HO, Ringsdorf H, Kornberg RD
Jazyk: angličtina
Zdroj: Biophysical journal [Biophys J] 1991 Feb; Vol. 59 (2), pp. 387-96.
DOI: 10.1016/S0006-3495(91)82232-9
Abstrakt: 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.
Databáze: MEDLINE