From the results of transformation experiments, the colour and fluorescence was used to identify colonies of XL-1 Blue E. coli cells that expressed GFP as a result of being transformed with the pQE30-GFP construct. The synthesis of GFP in cells transformed with the pQE30-GFP construct was induced with lactose analogue isopropyl ß-D-thiogalactopyranoside (IPTG) in larmmmmmge quantities. The bulk of the induced cells were then harvested and stored until later when the hexahistidine-tagged GFP protein was purified using IMAC (immobilised metal affinity chromatography) on nickel agarose. Plates from the 4°C cold-room were collected; the number and “type” of colony present on each plate was thus determined based on whether the colony expresses GFP (“+” GFP) or does not express GFP (“-“GFP). Thereafter, four overnight cultures of cells were setup, two from GFP producing colonies and two others from non GFP-producing colonies which were then inoculated. Finally an induction process was initiated after the tubes had stayed overnight whereby 1.5ml of each culture was set aside in microfuge tubes for later use. The LB was prepared to give a final concentration of 100μg/ml. 300µl of TENS buffer (TE/NaOH/SDS) was added to each tube;150µl of 3 M sodium acetate (pH 5.5) was also added to each tube; and finally, 0.9ml of ice-cold absolute ethanol was added and all were mixed at each interval. 200 µl of 70% (v/v) ethanol used to wash the DNA pellets. Each pellet was re-suspended in 50 µl OF TE. The plasmid DNA was then dissolved in 25µl of TE/RNase solution. Immediately after, a series of plasmid digest reactions in sterile microfuge tubes was set up for restriction digests of the same. Thereby, a control undigested sample was set aside. Finally, agarose electrophoresis of plasmid DNA restriction digests was carried out and the DNA bands viewed under UV light