Abstract
The emergence of multi-antibacterial resistant pathogens worldwide has become a crisis and new therapies are needed to combat this threat. One potential solution is the use of bacteriocins: bacterially produced polypeptides which killing competing species of bacteria. Here we describe an attempt to purify and determine the structure of putative bacteriocin receptor YthA. We successfully produced 320mg of inclusion bodies per litre of growth media, most of which was recombinant protein. Fusion protein precipitation caused the loss of much of the recovered fusion protein, though ultimately purification and refolding attempts were successful.