Crystallization and characterization of ribulose 1,5-bisphosphate carboxylase/oxygenase from eight plant species.
Ribulose bisphosphate carboxylase/oxygenase was isolated and crystallized from eight plant species. Crystals grew from either of two similar sets of crystallizing conditions: crystals of the enzyme from alfalfa, corn, cotton, potato, spinach, tobacco, and tomato grew from solutions containing phosphate and polyethylene glycol 6000 as a precipitant, and those from potato, tobacco (both Nicotiana sylvestris and Nicotiana tabacum), and tomato grew from a mixture of ammonium sulfate and phosphate. Crystals of the enzyme from potato and both species of tobacco were large enough to characterize by x-ray diffraction and were found to have the Form III structure, previously reported for crystals of ribulose bisphosphate carboxylase/oxygenase from N. tabacum. For crystalline material from several species, both carboxylase and oxygenase activites have been assayed and copper and iron contents have been determined. The possible significance of the observed general conditions of crystallization of this enzyme is discussed.
D002262:Carboxy-Lyases / Q000302:isolation & purification*; D003460:Crystallization; D003368:Gossypium / Q000201:enzymology; D000455:Medicago sativa / Q000201:enzymology; D010944:Plants / Q000201:enzymology*; D010947:Plants, Toxic; D011487:Protein Conformation; D012273:Ribulose-Bisphosphate Carboxylase / Q000302:isolation & purification*; D013045:Species Specificity; D014026:Nicotiana / Q000201:enzymology; D014961:X-Ray Diffraction
D002262:Carboxy-Lyases; D012273:Ribulose-Bisphosphate Carboxylase