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Atomic-force microscopy

Rhodopsin dimers in native disc membranes

Neat rows of paired photon receptors are caught on camera in their natural state.


In vertebrate retinal photoreceptors, the rod outer-segment disc membranes contain densely packed rhodopsin molecules for optimal light absorption and subsequent amplification by the visual signalling cascade1, but how these photon receptors are organized with respect to each other is not known. Here we use infrared-laser atomic-force microscopy to reveal the native arrangement of rhodopsin, which forms paracrystalline arrays of dimers in mouse disc membranes. The visualization of these closely packed rhodopsin dimers in native membranes gives experimental support to earlier inferences about their supramolecular structure2,3 and provides insight into how light signalling is controlled.

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Figure 1: Deflection image of a native eye-disc membrane adsorbed on mica, visualized by atomic-force microscopy (Nanoscope Multimode, Digital Instruments).
Figure 2: Organization and topography of the cytoplasmic surface of rhodopsin.


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Correspondence to Krzysztof Palczewski.

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The authors declare no competing financial interests.

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Fotiadis, D., Liang, Y., Filipek, S. et al. Rhodopsin dimers in native disc membranes. Nature 421, 127–128 (2003).

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