Long-range structural information provided by paramagnetic lanthanide probe methods is invaluable for the structural analysis of proteins, particularly protein complexes and multidomain proteins. The paramagnetic effects induced by the paramagnetic lanthanide ions fixed to the protein can be exploited to extract the distance and angular information of the observed nuclei with respect to the paramagnetic lanthanide ion. Indeed, application of paramagnetic lanthanide probes in protein structural analysis is expanding owing to the recent developments in lanthanide-binding tags. Here, we describe the paramagnetic effects that can be exploited to obtain the structural information of proteins. Additionally, we illustrate the practicality of experiments and analyses using paramagnetic lanthanide probe methods. We also highlight their applications in the structure determination of protein–protein complexes and visualization of conformational changes in multidomain proteins. Finally, we discuss further application of the paramagnetic lanthanide ions in integrated structural biology, especially exploiting electron spin resonance and solvent paramagnetic relaxation enhancement.