Crystallization and preliminary X-ray crystallographic studies of monoacylglycerol lipase of the moderately thermophilic Bacillus sp. H-257

Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1232-3. doi: 10.1107/s0907444902006169. Epub 2002 Jun 20.


Thermostable monoacylglycerol lipase (MGLP; EC 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus / enzymology*
  • Binding Sites
  • Crystallography, X-Ray / methods*
  • Hydrolysis
  • Monoacylglycerol Lipases / chemistry*
  • Protein Conformation
  • Temperature


  • Monoacylglycerol Lipases