The spin interaction that is usually employed for structural analyses via solid state NMR spectroscopy is the magnetic dipolar interaction.
Additional knowledge about other interactions within the studied system like the chemical shift or the electric quadrupole interaction can be helpful as well, and in some cases solely the chemical shift has been employed as e.g. for zeolites.
The “dipole coupling”-based approach parallels protein NMR spectroscopy to some extent in that e.g. multiple residual dipolar couplings are measured for proteins in solution, and these couplings are used as constraints in the protein structure calculation.
In NMR crystallography the observed spins in case of organic molecules would often be spin-1/2 nuclei of moderate frequency (, , , etc.). I.e.  is excluded due to its large magnetogyric ratio and high spin concentration leading to a network of strong homonuclear dipolar couplings. There are two solutions with respect to H:  spin diffusion experiments (see below) and specific labelling with  spins (spin = 1). The latter is also popular e.g. in NMR spectroscopic investigations of hydrogen bonds in solution and the solid state.
Both intra- and intermolecular structural elements can be investigated e.g. via deuterium REDOR (an established solid state NMR pulse sequence to measure dipolar couplings between deuterons and other spins).
This can provide an additional constraint for an NMR crystallographic structural investigation in that it can be used to find and characterize e.g. intermolecular hydrogen bonds.