Many halophilic bacteria and archaea are easy to maintain, and their high cellular osmotic pressure has been exploited in recombinant protein production. The cellular environments of halophiles can be fine-tuned to accommodate folding of protein of interest by adjusting the concentration of osmolytes in the culture medium. Successful expression and folding of Ice nucleation protein, GFP, α-amylase, nucleotide diphosphate kinase, and serine racemase have been reported in halophiles.[1]