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Literature DB >> 1901232

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

S A Darst¹, M Ahlers, P H Meller, E W Kubalek, R Blankenburg, H O Ribi, H Ringsdorf, R D Kornberg.

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.

Entities: Chemical

Mesh：

Substances：

Year: 1991 PMID： 1901232 PMCID： PMC1281155 DOI： 10.1016/S0006-3495(91)82232-9

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

11 in total

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6. Decreasing Transmembrane Segment Length Greatly Decreases Perfringolysin O Pore Size.

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