The 23 kDa two-domain periplasmic chaperone FIMC from Escherichia coli is required for the assembly of type-1 pili, which are filamentous, highly oligomeric protein complexes anchored to the outer bacterial membrane that mediate adhesion of pathogenic E. coli strains to host cell surfaces and persist in macrophages. Recombinant E. coli FIMC protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.