Fragment Based Drug Design (FBDD) is an established and successful method in the drug discovery and development process. Fragments are generally small, simple molecules with defined biophysical characteristics that, due to their small size usually bind to their target proteins with low binding affinity. Here we present the results of a fragment screening campaign against a 22 kDa bacterial thiol oxidoreductase enzyme (BpsDsbA). Efforts to generate a structure of the complex of BpsDsbA bound to a fragment were not successful. Therefore, and alternative approach was employed to determine the structure of a BpsDsbA bound to a fragment using solution NMR. This structural information will be used to guide the medicinal chemistry efforts to elaborate the fragment into a more potent and lead-like compound.