Recombinant Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein (chlL)

Recombinant Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein (chlL) can be expressed and purified from different hosts. E. coli and yeast offers the best yields and shorter turnaround times. Expression in insect cells with baculovirus or mammalian cells can provide many of the posttranslational modifications necessary for correct protein folding or retain the proteins activity.