In recent years the model of the Gram-negative bacterial cell envelope has changed. It is now understood that the outer membrane proteins exist within B-barrel protein arrays1. For the antimicrobial resistant pathogen Klebsiella pneumoniae the cell surface is an important contributor to its virulence and adaptability. This study sought to examine how membrane curvature at the cell poles influences the organisation of B-barrel protein arrays in Klebsiella. Minicells are small anucleate cells produced following aberrant cell division. Deletion or mutation of the minCDE operon that encodes the Min system, responsible for positioning the cell division machinery at the mid cell, results in cell division at the cell poles, producing minicells. Here, we present the characterisation of Klebsiella minicells and use them to interrogate outer membrane protein organisation in a membrane with tight curvature. Following the generation of the minCDE mutant in Klebsiella, biochemical analysis confirmed the presence of the inner and outer membranes in minicells. Fluorescence Activated Cell Sorting provided a robust method to purify minicells for further analysis. The curvature of the minicell membrane was examined using cryo-electron tomography and the radius of minicells determined using nanoparticle tracking analysis. The relative abundance of key outer membrane proteins was examined using proteomics and used to guide downstream determinations of absolute copy numbers. The information on cell curvature and outer membrane protein copy number was then used to calculate the geometry of a minicell and examine the relationship between the B-barrel arrays and the tightly curved membrane.