Abstract

We introduce a method for optically imaging intracellular proteins at nanometer spatial resolution. Numerous sparse subsets of photoactivatable fluorescent protein molecules were activated, localized (to ∼2 to 25 nanometers), and then bleached. The aggregate position information from all subsets was then assembled into a superresolution image. We used this method—termed photoactivated localization microscopy—to image specific target proteins in thin sections of lysosomes and mitochondria; in fixed whole cells, we imaged vinculin at focal adhesions, actin within a lamellipodium, and the distribution of the retroviral protein Gag at the plasma membrane.

Keywords

VinculinLamellipodiumMicroscopyActinSuperresolutionResolution (logic)Super-resolution microscopyPhotoactivated localization microscopyIntracellularBiophysicsCell biologyChemistryFluorescenceFluorescence microscopeFocal adhesionBiologyOpticsCytoskeletonBiochemistryCellPhysicsImage (mathematics)Computer science

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Publication Info

Year
2006
Type
article
Volume
313
Issue
5793
Pages
1642-1645
Citations
8649
Access
Closed

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Cite This

Eric Betzig, George H. Patterson, Rachid Sougrat et al. (2006). Imaging Intracellular Fluorescent Proteins at Nanometer Resolution. Science , 313 (5793) , 1642-1645. https://doi.org/10.1126/science.1127344

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DOI
10.1126/science.1127344