Paper Report for: Rengachari_2015_Acta.Crystallogr.F.Struct.Biol.Commun_71_243
Reference
Title: Purification, crystallization and preliminary X-ray diffraction analysis of a soluble variant of the monoglyceride lipase Yju3p from the yeast Saccharomyces cerevisiae Rengachari S, Aschauer P, Sturm C, Oberer M Ref: Acta Crystallographica F Struct Biol Commun, 71:243, 2015 : PubMed
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 A resolution. The crystal form was orthorhombic (space group P212121), with unit-cell parameters a = 77.2, b = 108.6, c = 167.7 A. The asymmetric unit contained four molecules with a solvent content of 46.4%.
Rengachari S, Aschauer P, Sturm C, Oberer M (2015) Purification, crystallization and preliminary X-ray diffraction analysis of a soluble variant of the monoglyceride lipase Yju3p from the yeast Saccharomyces cerevisiae Acta Crystallographica F Struct Biol Commun71: 243-6
Rengachari S, Aschauer P, Sturm C, Oberer M (2015) Acta Crystallographica F Struct Biol Commun71: 243-6