Crystallization and preliminary X-ray diffraction studies of tulip aryl acylamidase: a key enzyme in plant herbicide detoxification.
Crystals of aryl acylamidase (E.C. 3.5.1.13) from tulip bulbs have been obtained by the hanging-drop vapor-diffusion method using polyethylene glycol (PEG) 8000 as a precipitant. The crystals belong to space group P2(1)2(1)2(1) with unit-cell dimensions a = 68.7, b = 80.1 and c = 112.9 A. Assuming two molecules of molecular weight of 34 kDa in the asymmetric unit, V(m) is 2.28 A(3) Da(-1), indicating a solvent content of approximately 46%. The intensity data have been collected to 2.5 A resolution with an R(merge) of 0.067.
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
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Fukuda
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Matsumoto
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Hagiwara
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Fujimoto
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Mizuno