Integration in nanodiscs is a rather easy process. You can tune the size of the nanodiscs by engineering the MSP protein. If you adapt the size to the target protein then you might prevent integration of oligomers (unless the MP is already an oligomer natively). GPCRs go easily in nanodiscs, transporters a bit less and can be more problematic. Ion channels are fairly easy as well. What is more a concern is to do functional assay as you might have to find the right lipid combination and for eukaryiotic MPs you even might have to stabilize them. For structural studies (SAXS or NMR), I would say go for a tight nanodiscs (small one just slightly bigger than your protein) to decrease the all lability of the system.
So in conclusion, its definitely doable but it depends a bit on the stability of your target.
I would agree with Nicolas. The process of getting a good sample might take some optimisation, but it usually works. As long as you do not use the really large nano discs, you can feel relatively safe that you will only have one protein (monomer or whatever the native oligomeric state of your target protein is) per nano disc. There is simply not enough space in the smaller nano discs to fit much larger stuff in there.