Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules.
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.
Darst
S A
SA
Department of Cell Biology, Stanford University School of Medicine, California 94305.
Ahlers
M
M
Meller
P H
PH
Kubalek
E W
EW
Blankenburg
R
R
Ribi
H O
HO
Ringsdorf
H
H
Kornberg
R D
RD
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D001665:Binding Sites; D001710:Biotin / Q000378:metabolism; D016650:Fluorescein-5-isothiocyanate; D005452:Fluoresceins; D005456:Fluorescent Dyes; D008081:Liposomes; D008854:Microscopy, Electron; D008961:Models, Structural; D008968:Molecular Conformation; D011485:Protein Binding; D011487:Protein Conformation; D019809:Streptavidin; D013861:Thiocyanates
D001426:Bacterial Proteins; D005452:Fluoresceins; D005456:Fluorescent Dyes; D008081:Liposomes; D013861:Thiocyanates; D001710:Biotin; D019809:Streptavidin; D016650:Fluorescein-5-isothiocyanate