The Outer Membranes (OM) is a feature of many pathogenic bacteria. It is important as a barrier to antibiotics & the site of human-bacteria interaction. However bacteria are too small to allow us to do precise measurements of the structure and dynamics of this critical interface. Using neutrons as our eyes we have recently investigated OM models which imitate many aspects of the natural OM. Obtaining a dense protein containing version of the OM model has its own challenges and we have been developing a system where OmpF protein is assembled on gold surfaces so that it is 100% oriented .The spaces between are filled with deuterated decane thiol and LPS on the outer surface. Here we want to extend our study of the important antibiotic PMB. Previous work at ISIS clarified the interaction with lipids and now we wish to understand how proteins alter PMB's mode of action.