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Article Abstract
F ENDOR is emerging as a powerful tool in structural biology for measuring distances in proteins labeled with F and a paramagnetic tag. Due to spin-spin relaxation and line width limitations, it has been difficult to determine intertag distances larger than about 15 Å. Using a set of geometrically well-defined rulers and spin-labeled proteins, we show that F-Gd distances up to 20 Å can be accessed by integrating the intensity of the ENDOR spectrum, with distances approaching 30 Å potentially in reach as well. This method is robust when the intensities are scaled to a known reference, and provides scope for nanometer-scale triangulation of the coordinates of a ligand in a protein-ligand complex.
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| http://dx.doi.org/10.1021/jacs.4c13530 | DOI Listing |
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