Magic-angle-spinning nuclear magnetic resonance (NMR) is ideal for studying protein structure and dynamics. Introducing fluorine atoms offers advantages due to the NMR properties of ¹⁹F and the absence of natural fluorine. However, the slow spin polarisation recovery of ¹⁹F causes long recycle delays between scans. We demonstrate that adding paramagnetic co-solutes to solid protein samples largely accelerates these experiments, and we identify optimal conditions for this approach.