CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF TULIP ARYL ACYLAMIDASE - A KEY ENZYME IN PLANT HERBICIDE DETOXIFICATION

Authors
FUKUDA K MATSUMOTO T HAGIWARA K FUJIMOTO Z MIZUNO H
Citation
K. Fukuda et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF TULIP ARYL ACYLAMIDASE - A KEY ENZYME IN PLANT HERBICIDE DETOXIFICATION, Acta crystallographica. Section D, Biological crystallography, 53, 1997, pp. 342-344
Citations number
16
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
53
Year of publication
1997
Part
3
Pages
342 - 344
Database
ISI
SICI code
0907-4449(1997)53:<342:CAPDSO>2.0.ZU;2-F
Abstract
Crystals of aryl acylamidase (E.C. 3.5.1.13) from tulip bulbs have bee n obtained by the hanging-drop vapor-diffusion method using polyethyle ne glycol (PEG) 8000 as a precipitant. The crystals belong to space gr oup P2(1)2(1)2(1) with unit-cell dimensions a = 68.7, b = 80.1 and c = 112.9 Angstrom. Assuming two molecules of molecular weight of 34 kDa in the asymmetric unit, V-m is 2.28 Angstrom 3 Da(-1) indicating a sol vent content of approximately 46%. The intensity data have been collec ted to 2.5 Angstrom resolution with an R-merge of 0.067.