Solid-state NMR is a promising method for structural analysis of membrane proteins. The method is capable of providing atomic-resolution structure information without the need for crystals or fast molecular motion as is required for X-ray diffraction and liquid-state NMR, respectively. However, it is clear that solid-state NMR still needs substantial methodological development before it can provide the desired detailed information about large structures or be applied routinely for structure-function relationship studies. Here, we address some important considerations and elements in the solid-state NMR methodology relevant for characterization of membrane proteins. These are relevant for establishing the appropriate technology and may serve as an inspiration for future developments in synthesis, isotope labeling, and physical preparation of samples for solid-state NMR characterization. textcopyright 2003 Wiley Periodicals, Inc.