In the last few years it has been demonstrated that membrane proteins can be successfully reconstituted into small membrane-like devices termed Nanodiscs. Consisting of a 10-14 nm sized phospholipid bilayer stabilized by an amphipatic protein belt, MSP, the Nanodisc stabilizes the membrane protein by providing a native-like environment. Considerable insight into the structural organization of the Nanodisc has been obtained by our group in previous experiments at ILL and ESRF through a combined SANS/SAXS approach. These data have enabled us to start optimizing the Nanodisc-carrier to be used as a platform for structural studies of membrane proteins in solution. The latest development of the system is the construction of a selectively deuterated and contrast minimized Nanodisc carrier, done in close collaboration with the D-LAB, Grenoble. This stealth nanodisc-carrier will then, relatively, enhance the neutron signal from the incorporated membrane protein, which is the system in focus. The aim of this proposed experiment is to establish the proof-of-concept of this stealth Nanodiscs approach to investigate membrane proteins.