In recent years, a large number of solid–state nuclear magnetic resonance (NMR) techniques have been developed and applied to the study of fully or significantly isotopically labelled ( ¹³ C, ¹⁵ N or ¹³ C/ ¹⁵ N) biomolecules. In the past few years, the first structures of ¹³ C/ ¹⁵ N–labelled peptides, Gly–Ile and Met–Leu–Phe, and a protein, Src–homology 3 domain, were solved using magic–angle spinning NMR, without recourse to any structural information obtained from other methods. This progress has been made possible by the development of NMR experiments to assign solid–state spectra and experiments to extract distance and orientational information. Another key aspect to the success of solid–state NMR is the advances made in sample preparation. These improvements will be reviewed in this contribution. Future prospects for the application of solid–state NMR to interesting biological questions will also briefly be discussed.