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Title
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Preliminary crystallographic data for stearoyl-acyl carrier protein desaturase from castor seed.
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Authors
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G.Schneider,
Y.Lindqvist,
J.Shanklin,
C.Somerville.
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Ref.
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J Mol Biol, 1992,
225,
561-564.
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PubMed id
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Abstract
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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.
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