Bacterial outer membrane proteins are factors critical in host-pathogen interactions, but understanding the biogenesis of these proteins has been a technological challenge. The BAM complex mediates this process and we have been working to establish experimental systems in membrane environments to determine the architecture and measure the activity of the BAM complex. We have imaged the BAM complex in a membrane environment using super-resolution microscopy, and used in situ cross-linking in live Escherichia coli to map the interactions between BamA, BamB, BamC and the other subunits through a reaction cycle driven by the addition of a substrate protein. These experimental systems demonstrate substantial movements in the BAM complex in and out of the membrane as being crucial to the mechanism of bacterial membrane protein assembly, and suggest unexpected mechanistic parallels to classic molecular chaperones such as the bacterial GroEL/GroES complex. An exciting and recent report of a small molecule inhibitor of the BAM complex is now being assayed in these systems. The ancillary module of the beta-barrel assembly machinery, the TAM, has also being characterized and shown to be of particular importance in the assembly of fimbrial usher proteins and, therefore, critical for the rapid deployment of fimbriae by bacterial pathogens.