Integral membrane proteins (IMPs) are usually extracted from their native lipid environment by detergent solubilisation in order to be used for structural studies. SAXS and SANS studies of membrane proteins in detergent micelles are problematic due to the dominating contribution of detergent and background scattering of empty micelles. Reconstitution of IMPs in nanodiscs can overcome these obstacles and allow low-resolution structural investigation in membrane proteins in a native-like solution environment. In order to fully contrast-match-out the nanodisc carriers, we plan to incorporate our IMP targets in stealth carriers consisting of deuterated MSP1 belt protein and deuterated lipids. This would allow the low-resolution structural characterization of our IMPs of interest in a native-like lipid environment without nanodisc contribution.