title: Crystallization and preliminary X-ray diffraction analysis of salutaridine reductase from the opium poppy Papaver somniferum.
abstract: The opium poppy Papaver somniferum is the source of the narcotic analgesics morphine and codeine. Salutaridine reductase (SalR; EC 1.1.1.248) reduces the C-7 keto group of salutaridine to the C-7 (S)-hydroxyl group of salutaridinol in the biosynthetic pathway that leads to morphine in the opium poppy plant. P. somniferum SalR was overproduced in Escherichia coli and purified using cobalt-affinity and size-exclusion chromatography. Hexagonal crystals belonging to space group P6(4)22 or P6(2)22 were obtained using ammonium sulfate as precipitant and diffracted to a resolution of 1.9 A.
authors.affiliation: Donald Danforth Plant Science Center, 975 North Warson Road, St Louis, Missouri 63132, USA. yhigashi@danforthcenter.org
authors.forename: Yasuhiro
authors.initials: Y
authors.lastname: Higashi
authors.forename: Thomas J
authors.initials: TJ
authors.lastname: Smith
authors.forename: Joseph M
authors.initials: JM
authors.lastname: Jez
authors.forename: Toni M
authors.initials: TM
authors.lastname: Kutchan
mesh_terms: D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003460:Crystallization; D010088:Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D010207:Papaver / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D010088:Oxidoreductases; C520720:salutaridine reductase, Papaver