Cells and organelles are enclosed by lipid bilayers that separate them from their external environment. Embedded in these membranes are particular proteins that span the full width of the bilayer and mediate communication between the two sides. These membrane proteins carry out a multitude of tasks and adopt different architectures, ranging from single transmembrane‐spanning domains to large multimeric assemblies. Although membrane proteins constitute more than 30% of known proteins, they represent less than 1% of the high‐resolution protein structures deposited in the Protein Data Bank. Their hydrophobicity and their dependence on lipids render them difficult to crystallize and to purify in a soluble form. Recent developments performed in solid‐state NMR spectroscopy offer unique opportunities to address such systems on the atomic level in their native environment. Indeed, membrane proteins have been the subject of solid‐state NMR for more than three decades, and pioneering studies on bacteriorhodopsin [ 1-3] and gramicidin [ 4] have established its utility in studying molecules that are otherwise untenable with other structural tools. In recent years, it has also become clear that solid‐state NMR is capable of delivering comprehensive information about larger membrane proteins, including retinal proteins, ion channels, membrane‐embedded enzymes [ 5-7], histidine kinases [ 8], ATP‐binding cassette transporters [ 9], bacterial outer membrane proteins [ 10, 11], and G‐protein‐coupled receptors [ 12, 13]. In this chapter, we introduce some of the preparatory and experimental aspects to investigate integral membrane proteins by high‐resolution solid‐state NMR spectroscopy. Furthermore, we consider methodological approaches that deliver structural parameters from solid‐state NMR data of membrane proteins with particular attention to retinal proteins and ion channels.