Abstract
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 12 12 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 Å 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 ° intervals, i.e. maxima at κ = 180 °, φ = 90 ° and ω = 30 ° and 60 °, respectively. Together with the packing density of the crystals ( V m = 2.4 Å) 3/Da for n = 6), these results suggest, that the crystal asymmetric unit most likely contains a hexamer of desaturase subunits.
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