Imaging streptavidin 2D crystals on biotinylated lipid monolayers at high resolution with the atomic force microscope.

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Bibliographic Details
Title:	Imaging streptavidin 2D crystals on biotinylated lipid monolayers at high resolution with the atomic force microscope.
Authors:	SCHEURING, S¹, MÜLLER, D. J¹, RINGLER, P¹, HEYMANN, J. B¹, ENGEL, A¹
Source:	Journal of Microscopy. Jan1999, Vol. 193 Issue 1, p28-35. 8p. 11 Black and White Photographs, 4 Diagrams, 1 Chart.
Subjects:	Streptavidin, Crystals, Electron microscopy, Atomic models, X-ray crystallography
Abstract:	Streptavidin crystals were grown on biotinylated lipid monolayers at an air/water interface and transferred onto highly oriented pyrolytic graphite (HOPG). These arrays could be imaged to a resolution below 1 nm using the atomic force microscope. The surface topographs obtained were compared with negative-stain electron microscopy images and the atomic model as determined by X-ray crystallography. The streptavidin tetramer (60 kDa) exposes two free biotin-binding sites to the buffer solution, while two are occupied by linkage to the lipid monolayer. Therefore, the streptavidin 2D crystals can be used as nanoscale matrices for binding biotinylated compounds. Furthermore, this HOPG-based preparation method provides a general novel approach to study the structure of protein arrays assembled on lipid monolayers with the AFM. [ABSTRACT FROM AUTHOR]
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Database:	Engineering Source

Description
Abstract:	Streptavidin crystals were grown on biotinylated lipid monolayers at an air/water interface and transferred onto highly oriented pyrolytic graphite (HOPG). These arrays could be imaged to a resolution below 1 nm using the atomic force microscope. The surface topographs obtained were compared with negative-stain electron microscopy images and the atomic model as determined by X-ray crystallography. The streptavidin tetramer (60 kDa) exposes two free biotin-binding sites to the buffer solution, while two are occupied by linkage to the lipid monolayer. Therefore, the streptavidin 2D crystals can be used as nanoscale matrices for binding biotinylated compounds. Furthermore, this HOPG-based preparation method provides a general novel approach to study the structure of protein arrays assembled on lipid monolayers with the AFM. [ABSTRACT FROM AUTHOR]
ISSN:	00222720
DOI:	10.1046/j.1365-2818.1999.00434.x