title: Crystallization and preliminary X-ray crystallographic studies of monoacylglycerol lipase of the moderately thermophilic Bacillus sp. H-257.
abstract: Thermostable monoacylglycerol lipase (MGLP; EC 3.1.1.23) from the moderately thermophilic Bacillus sp. H-257 has a unique substrate specificity. It hydrolyzes monoacylglycerols but does not hydrolyze di- or triacylglycerols. Crystals of the enzyme were obtained by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant and benzamidine as an additive. The orthorhombic crystals belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 43.53, b = 100.82, c = 108.17 A. The crystals diffract to at least 2.3 A resolution and a native data set has been collected to 2.6 A resolution on a CCD detector using synchrotron radiation.
authors.affiliation: Institute for Health Sciences, Tokushima Bunri University, Yamashiro-cho, Japan.
authors.forename: Kazunari
authors.initials: K
authors.lastname: Yoneda
authors.forename: Tomohiro
authors.initials: T
authors.lastname: Nishimura
authors.forename: Nobuhiko
authors.initials: N
authors.lastname: Katunuma
authors.forename: Shigeyuki
authors.initials: S
authors.lastname: Imamura
authors.forename: Katsutoshi
authors.initials: K
authors.lastname: Nitta
authors.forename: Hideaki
authors.initials: H
authors.lastname: Tsuge
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D001665:Binding Sites; D018360:Crystallography, X-Ray / Q000379:methods*; D006868:Hydrolysis; D008994:Monoacylglycerol Lipases / Q000737:chemistry*; D011487:Protein Conformation; D013696:Temperature
chemical_list: D008994:Monoacylglycerol Lipases