Due to numerous achievements in the last years, solid-state NMR has evolved a potent tool for structural characterization of biomolecules. Not relying on single crystals or solubility, the technique particularly focuses on fibrillar and membrane proteins, which are difficult to characterize otherwise. Despite this enormous potential, numerous difficulties unsolved to date demand for further technical and methodological reworking. Among these, the achievable signal to noise and resolution are the most prominent limits. Whereas a series of limitations is induced by strong dipolar interactions...