Abstract
Bacteriorhodopsin (bR) is one of the best studied transport proteins, having been first purified in 1974 by Oesterhelt and Stoeckenius. Acting as a proton pump in halophilic archaea, bR forms crystalline patches in the cell membrane of about 100 nm in size. Despite decades of research into bR, the purpose of these crystalline patches is widely unknown. To determine what benefit patches offer the cell, a method is needed that can measure the activity of bR with sub-diffraction limited resolution.
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