The proteins of the outer membrane of Gram-negative bacteria are critical for bacterial survival,from providing basic physiological functions, to impairing virulence and multidrug resistance. The Bam complex has been found to be essential for folding these proteins into the outer membrane.The process by which this is achieved is unknown. The structure of the complex and its individual components are now known. We aim to continue our investigation of the Bam complex by studying BamABCDE in complex with stalled folding intermediates. To do this we will use specific deuteration and neutron reflectometry in concert with previous PNR datasets of the BamABCDE complex bound to a gold surface to probe the structure of the Bam complex as it performs its function.