The proteins of the outer membrane of Gram-negative bacteria are critical for bacterialsurvival, from providing basic physiological functions, to aiding virulence and multidrugresistance. The Bam complex has been found to be essential for folding these proteins intothe outer membrane. The process by which this is achieved is unknown. Key to thisunderstanding is the knowledge of the structure of the complex and its individualcomponents. We aim to continue our investigation of the Bam complex by studying the complete BamABCDE complex and in particular identify how the individual components are organised on the membrane surface. To do this will use neutron reflectometry and specific deuteration to probe the structure of the Bam complex in a model E.coli outer membrane and elucidate the scaffolding of this essential complex on the membrane surface for the first time.