A novel hybrid approach for the structure calculations of membrane proteins using restraints derived from solution and solid-state NMR will be presented. This hybrid method combines restraints from solution NMR experiments carried out in detergent micelles (nuclear Overhauser effects, paramagnetic relaxation enhancements, residual dipolar couplings, and 3J couplings) with anisotropic parameters derived from solid-state NMR in oriented DOPC/DOPE lipid bilayers (1H-15N dipolar couplings and 15N chemical shift anisotropy) for the simultaneous determination of high-resolution structure and topology of membrane proteins. All of the structural restraints are incorporated into a single structural refinement protocol using XPLOR-NIH software. We show the application of this method to phospholamban (PLN), a pentameric integral membrane protein involved in muscle contraction and relaxation. We propose this approach as a general method for structure determination of membrane proteins at high-resolution.