As Prof. K. W??thrich stated, the NMR spectroscopy is one of the principal experimental techniques of structural biology. It has the abilities to determine structures at atomic resolution as well as investigate dynamics and intermolecular interactions of biological macromolecules. The combination of stable isotope (13C15N) labelling and advanced multinuclear NMR techniques has made NMR a complementary method to X-ray crystallography in structural biology. Roughly 15-20% of the structures of biological macromolecules determined in the past few years were obtained by using the NMR spectroscopy.

Unfortunately, although dozens of high field NMR machines have been installed in the mainland of China during the past ten years, none of the NMR structures of double-labelled protein has been reported. The NMR group led by Prof. Shi Yunyu has now succeeded in the 13C15N-labelling of protein and implementation of sophisticated heteronuclear triple-resonance NMR experiments on their Bruker 500MHz NMR spectrometer.

Several biologically important proteins are now under investigation. Among them, the NMR structure of hUBF (human upstream binding factor) box1 has been obtained (99 residues); the investigation on the interaction of box1 with DNA by NMR is going on. The 1H, 13C, and 15N resonance assignment of another transcription factor ADR6 (115 residues) has been published in Journal of Biomolecular NMR; the structural refinement will be finished soon. The NMR work on human VHR (vaccinia H1-related phosphatase, 192 residues) has begun.