Crystallization and preliminary X-ray diffraction studies of tulip aryl acylamidase: a key enzyme in plant herbicide detoxification
Acta Crystallographica Section D
Volume 53, Issue 3, pages 342–344, May 1997
How to Cite
Fukuda, K., Matsumoto, T., Hagiwara, K., Fujimoto, Z. and Mizuno, H. (1997), Crystallization and preliminary X-ray diffraction studies of tulip aryl acylamidase: a key enzyme in plant herbicide detoxification. Acta Crystallographica Section D, 53: 342–344. doi: 10.1107/S0907444996015363
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Crystals of aryl acylamidase (E.C. 184.108.40.206) 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 P212121 with unit-cell dimensions a = 68.7, b = 80.1 and c = 112.9 Å. Assuming two molecules of molecular weight of 34 kDa in the asymmetric unit, Vm is 2.28 Å3 Da−1, indicating a solvent content of approximately 46%. The intensity data have been collected to 2.5 Å resolution with an Rmerge of 0.067.