An important achievement of the scientific community, therefore, has been the development of technologies that allow the high throughput expression of recombinant proteins. These In Vitro Transcription and Translation systems (IVTT) or cell-free systems offer several advantages over traditional cell-based expression methods and are suitable for high throughput strategies due to reduced reaction volumes and process time [4, 5, 6] . Additional advantages include easy modification of reaction conditions for improving production of complex proteins, decreased sensitivity to product toxicity, and high yield. Importantly, cell-free systems have proved capable of generating proteins from complex parasites that have been difficult to produce in traditional cell-based systems, such as Plasmodium proteins [7, 8, 9, 10] . The most efficient expression to date has been achieved with an E. coli cell-free system which has yielded more than 93% efficiency of expression with a panel of 250 P. falciparum (Pf) proteins [11] . Eukaryotic based cell-free systems are also available with wheat germ, rabbit reticulocytes and insect cells. The eukaryotic lysate is considered by some to provide a better platform for production of complex proteins particularly with regard to post-translational modifications. Recently, up to 75% efficiency of production of Pf proteins in the wheat germ system has been reported [12, 13] but this is still less efficient than that observed with the E. coli system [11] .