Preliminary crystallographic data for stearoyl-acyl carrier protein desaturase from castor seed.
Recombinant stearoyl-acyl carrier protein desaturase (EC 1.14.99.6) from castor seed has been crystallized with polyethylene glycol 8000 as precipitant. The crystals are orthorhombic, space group P2(1)2(1)2(1) with cell dimensions a = 81.3, b = 146.4 and c = 197.7 A. The observed diffraction pattern extends to at least 2.5 A resolution. Rotation function calculations indicate a non-crystallographic 3-fold rotation axis parallel to the crystallographic a-axis. Perpendicular to this axis, 2-fold rotation axes were found at 30 degrees intervals, i.e. maxima at kappa = 180 degrees, phi = 90 degrees and omega = 30 degrees and 60 degrees, respectively. Together with the packing density of the crystals (Vm = 2.4 A3/Da for n = 6), these results suggest, that the crystal asymmetric unit most likely contains a hexamer of desaturase subunits.
Schneider
G
G
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.
Lindqvist
Y
Y
Shanklin
J
J
Somerville
C
C
D003460:Crystallization; D046911:Macromolecular Substances; D006899:Mixed Function Oxygenases / Q000737:chemistry*; D010944:Plants / Q000201:enzymology; D011092:Polyethylene Glycols; D011994:Recombinant Proteins / Q000737:chemistry; D012639:Seeds / Q000201:enzymology*; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D011994:Recombinant Proteins; D011092:Polyethylene Glycols; D006899:Mixed Function Oxygenases; C018747:acyl-(acyl-carrier-protein)desaturase