Folates are ubiquitous in rapidly dividing cells as found in the malaria parasite and little is known about the folate pathway in Plasmodium compared to the same pathway in the human host. The co-expression of the molecular chaperone, PfHsp70 with PfGCHI improved the production of the latter in E. coli. The fact that PfGCHI was produced as soluble and active protein is of importance towards its characterisation as a potential antimalarial drug target. A putative structure for PfGCHI would greatly aid the design of drugs specific to PfGCHI.