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. 1990 Dec;58(6):1473–1480. doi: 10.1016/S0006-3495(90)82492-9

Imaging the membrane protein bacteriorhodopsin with the atomic force microscope.

H J Butt 1, K H Downing 1, P K Hansma 1
PMCID: PMC1281099  PMID: 2275963

Abstract

The membrane protein bacteriorhodopsin was imaged in buffer solution at room temperature with the atomic force microscope. Three different substrates were used: mica, silanized glass and lipid bilayers. Single bacteriorhodopsin molecules could be imaged in purple membranes adsorbed to mica. A depression was observed between the bacteriorhodopsin molecules. The two dimensional Fourier transform showed the hexagonal lattice with a lattice constant of 6.21 +/- 0.20 nm which is in agreement with results of electron diffraction experiments. Spots at a resolution of approximately 1.1 nm could be resolved. A protein, cationic ferritin, could be imaged bound to the purple membranes on glass which was silanized with aminopropyltriethoxysilane. This opens the possibility of studying receptor/ligand binding under native conditions. In addition, purple membranes bound to a lipid bilayer were imaged. These images may help in interpreting results of functional studies done with purple membranes adsorbed to black lipid membranes.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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