Rotational resonance is a solid-state NMR method for restoring homonuclear dipolar couplings in magic angle spinning (MAS) experiments. Measurements of dipolar couplings can be used to determine internuclear distances which in turn provide direct constraints on molecular structure. The dipolar coupling between two spins is estimated from the observed intensity changes in a magnetization exchange experiment carried out while spinning the sample at a rotational resonance condition, i.e. when Delta = n omega(r), where Delta is the difference in chemical shift of two dipole-coupled spins, omega(r) is the rotational frequency in the MAS experiment, and n is a small integer corresponding to the rotational resonance order. Rotational resonance NMR data and calculations are presented for a crystalline 11-residue peptide incorporating pairs of C-13 labels separated by 3.7, 4.5, 4.8, 5.1, and 6.8 Angstrom. We discuss the critical parameters in generating and interpreting the magnetization exchange curves that are used to relate the observed intensity changes in the rotational resonance spectra to dipolar couplings. The accuracy of internuclear distance estimates from these experiments depends on the precision of the measurements as well as correctly accounting for natural abundance background signals, the effects of proton B-1 field strengths, and inhomogeneous broadening of the dipole-coupled NMR resonances. For the crystalline 11-residue peptide, the precision and accuracy of the RR distance measurements are on the order of 0.1 and 0.2-0.3 Angstrom, respectively. On the basis of these studies, we outline approaches for determining internuclear distances in both crystalline and non-crystalline solid-state samples.