A method for expressing proteins as a fusion chimera with a domain of p26
or alpha crystallin type proteins to improve the protein stability and
solubility when over expressed in bacteria such as E. coli is provided.
Genes of interest are cloned into the multiple cloning site of the Vector
System just downstream of the p26 or alpha crystallin type protein and a
thrombin cleavage site. Protein expression is driven by a strong
bacterial promoter (TAC). The expression is induced by the addition of 1
mM IPTG that overcomes the lac repression (lac I.sub.q). The soluble
recombinant protein is purified using a fusion tag.