The Beta-barrel assembly machinery (BAM) is essential for localization and function of the vast majority of cell surface proteins on bacterial cells. We developed a direct stochastic optical reconstruction microscopy (dSTORM) methodology and used video-rate, single-molecule localization microscopy to view the BAM complex in situ. Further, we believe the auxiliary lipoprotein subunit BamB is crucial for this spatial distribution. Statistical analysis showed that the BAM complex clusters grow when outer membrane protein synthesis is maximal, visual proof that the precincts are active in protein assembly. This nanoscale interrogation of the BAM complex in situ suggests a new model whereby bacterial outer membranes contain highly organized assembly precincts to drive integral protein assembly.