Purification, crystallization and preliminary X-ray diffraction analysis of a soluble variant of the monoglyceride lipase Yju3p from the yeast Saccharomyces cerevisiae

Acta Crystallogr F Struct Biol Commun. 2015 Feb;71(Pt 2):243-6. doi: 10.1107/S2053230X15001557. Epub 2015 Jan 28.


The protein Yju3p is the orthologue of monoglyceride lipases in the yeast Saccharomyces cerevisiae. A soluble variant of this lipase termed s-Yju3p (38.3 kDa) was generated and purified to homogeneity by affinity and size-exclusion chromatography. s-Yju3p was crystallized in a vapour-diffusion setup at 293 K and a complete data set was collected to 2.4 Å resolution. The crystal form was orthorhombic (space group P212121), with unit-cell parameters a = 77.2, b = 108.6, c = 167.7 Å. The asymmetric unit contained four molecules with a solvent content of 46.4%.

Keywords: monoacylglycerol lipase; monoglyceride lipase; s-Yju3p.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Chromatography, Gel
  • Crystallization
  • Electrophoresis, Polyacrylamide Gel
  • Molecular Sequence Data
  • Monoacylglycerol Lipases / chemistry*
  • Monoacylglycerol Lipases / isolation & purification*
  • Protein Isoforms / chemistry
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / isolation & purification*
  • Solubility
  • X-Ray Diffraction*


  • Protein Isoforms
  • Saccharomyces cerevisiae Proteins
  • Monoacylglycerol Lipases
  • Yju3 protein, S cerevisiae