Paramagnetic Properties of a Crystalline Iron-Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy.We present the first solid-state NMR study of an iron-sulfur protein.  For these residues, contact shifts as large as 100 and 400 ppm for 1H and 13C resonances, respectively, were observed, which represent the most shifted solid-state NMR signals ever measured in metalloproteins. 
NMR
Paramagnetic Properties of a Crystalline Iron-Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy.We present the first solid-state NMR study of an iron-sulfur protein. 
Magic-Angle Spinning NMR Spectroscopy