The lack of antibiotic development coupled with the rapid increase of resistance to antibiotics in bacteria, has led to a situation described by the Infectious Disease Society of America as an ‘alarming public health crisis’. Multi-drug resistant (MDR) bacteria are becoming a significant problem as some bacterial strains cannot be treated with our current strongest and last resort antibiotics. There is an urgent need to develop alternative strategies to combat these bacterial infections. MDR bacteria include two Neisseria species: N. meningitidis, the causative agent of meningitis, and N. gonorrhoeae, which cause sexually transmitted gonorrhoea. The overall aim of this work is to develop a narrow spectrum antibiotic against N. meningitidis. The biological target: NmDsbD, is a disulfide bond (Dsb) reductase that is required for the viability of N. meningitidis. NmDsbD is membrane bound and consists of three redox active domains: two are periplasmic domains, n-NmDsbD and c-NmDsbD, which flank the transmembrane domain, t-NmDsbD. In this study, the initial biochemical characterisation of n-NmDsbD and c-NmDsbD were carried out and the crystal structures of these domains were solved to 2.5 Å and 2.3 Å, respectively.