The crystals of PatF are grown from recombinant PatFprotein. The protein is overexpressed in lab strains of E. coli cultured in Formedium LB broth supplemented with antibiotics. The recombinant PatF protein is purified away from the cocktail of endogenous E. coli proteins using column chromatography.
PatF from Prochloron didemni is made up of a beta barrel core surrounded on the outside by alpha helices in a TIM-barrel like conformation. The protein is a member of the cyanobactin prenyl transferase class but has been found through sequence variation in the active site to be evolutionary inactive.
Structure of PatF from Prochloron didemni. Bent, Andrew F; Koehnke, Jesko; Houssen, Wael E; Smith, Margaret C M; Jaspars, Marcel; Naismith, James H. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 69, No. 6, 06.2013, p. 618-623.
Thank you to Andrew Bent, University of St Andrews for supplying the images and descriptions.