Yoneda_2002_Acta.Crystallogr.D.Biol.Crystallogr_58_1232

Reference

Title : Crystallization and preliminary X-ray crystallographic studies of monoacylglycerol lipase of the moderately thermophilic Bacillus sp. H-257 - Yoneda_2002_Acta.Crystallogr.D.Biol.Crystallogr_58_1232
Author(s) : Yoneda K , Nishimura T , Katunuma N , Imamura S , Nitta K , Tsuge H
Ref : Acta Crystallographica D Biol Crystallogr , 58 :1232 , 2002
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.

PubMedSearch : Yoneda_2002_Acta.Crystallogr.D.Biol.Crystallogr_58_1232
PubMedID: 12077453
Gene_locus related to this paper: bac25-mglp

Related information

Gene_locus bac25-mglp
Structure bac25-mglp    4LHE

Citations formats

Yoneda K, Nishimura T, Katunuma N, Imamura S, Nitta K, Tsuge H (2002)
Crystallization and preliminary X-ray crystallographic studies of monoacylglycerol lipase of the moderately thermophilic Bacillus sp. H-257
Acta Crystallographica D Biol Crystallogr 58 :1232

Yoneda K, Nishimura T, Katunuma N, Imamura S, Nitta K, Tsuge H (2002)
Acta Crystallographica D Biol Crystallogr 58 :1232