Site-specific assignments for the solid-state NMR spectra of uniformly C-13, N-15-enriched ubiquitin are described. The assignments are derived from three three-dimensional N-15-C-13-C-13 correlation spectra collected at 400 MHz on microcrystalline material. A few residues (the loop near Threonine 9 and the C-terminal fragment) were missing and correspond to regions previously reported to be mobile on the basis of X-ray crystallography and solution NMR studies. A few additional sites exhibit shifts that differ from previously reported solution NMR assignments. Nonetheless, these de novo assignments indicate close agreement between the chemical shifts observed in solution and those in microcrystalline or precipitated solids. The methods utilized are likely to be generally applicable for other noncrystalline, nonsoluble proteins.