The ability to simultaneously measure many long-range distances is critical to efficient and accurate determination of protein structures by solid-state NMR (SSNMR). So far, the most common distance constraints for proteins are C-N distances, which are usually measured using the rotational-echo double-resonance (REDOR) technique. However, these measurements are restricted to distances of up to ~ 5 Å due to the low gyromagnetic ratios of N andC. Here we present a robust 2D C-F REDOR experiment to measure multiple distances to ~ 10 Å. The technique targets proteins that contain a small number of recombinantly or synthetically incorporated fluorines. The C-F REDOR sequence is combined with 2D C-C correlation to resolve multiple distances in highly C-labeled proteins. We show that, at the high magnetic fields which are important for obtaining well resolvedC spectra, the deleterious effect of the large F chemical shift anisotropy for REDOR is ameliorated by fast magic-angle spinning and is further taken into account in numerical simulations. We demonstrate this 2DC-C resolved C-F REDOR technique on C,N-labeled GB1. A 5-F-Trp tagged GB1 sample shows the extraction of distances to a single fluorine atom, while a 3-F-Tyr labeled GB1 sample allows us to evaluate the effects of multi-spin coupling and statistical F labeling on distance measurement. Finally, we apply this 2D REDOR experiment to membrane-bound influenza B M2 transmembrane peptide, and show that the distance between the proton-selective histidine residue and the gating tryptophan residue differs from the distances in the solution NMR structure of detergent-bound BM2. This 2DC-F REDOR technique should facilitate SSNMR-based protein structure determination by increasing the measurable distances to the ~ 10 Å range.