The F-19 chemical shift is a sensitive NMR probe of structure and electronic environment in organic and biological molecules. In this report, we examine chemical shift parameters of 4F-, 5F-, 6F-, and 7F-substituted crystalline tryptophan by magic angle spinning (MAS) solid-state NMR spectroscopy and density functional theory. Significant narrowing of the 19F lines was observed under fast MAS conditions, at spinning frequencies above 50 kHz. The parameters characterizing the 19F chemical shift tensor are sensitive to the position of the fluorine in the aromatic ring and, to a lesser extent, the chirality of the molecule. Accurate calculations of F-19 magnetic shielding tensors require the PBEO functional with a 50% admixture of a Hartree Fock exchange term, as well as taking account of the local crystal symmetry. The methodology developed will be beneficial for 19F based MAS NMR structural analysis of proteins and protein assemblies.