Crystallization and preliminary X-ray crystallographic studies of monoacylglycerol lipase of the moderately thermophilic Bacillus sp. H-257.
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.
Yoneda
Kazunari
K
Institute for Health Sciences, Tokushima Bunri University, Yamashiro-cho, Japan.
Nishimura
Tomohiro
T
Katunuma
Nobuhiko
N
Imamura
Shigeyuki
S
Nitta
Katsutoshi
K
Tsuge
Hideaki
H
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
D008994:Monoacylglycerol Lipases