| Title : Purification, crystallization and preliminary X-ray diffraction analysis of a soluble variant of the monoglyceride lipase Yju3p from the yeast Saccharomyces cerevisiae - Rengachari_2015_Acta.Crystallogr.F.Struct.Biol.Commun_71_243 |
| Author(s) : Rengachari S , Aschauer P , Sturm C , Oberer M |
| Ref : Acta Crystallographica F Struct Biol Commun , 71 :243 , 2015 |
|
Abstract :
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%. |
| PubMedSearch : Rengachari_2015_Acta.Crystallogr.F.Struct.Biol.Commun_71_243 |
| PubMedID: 25664804 |
| Gene_locus related to this paper: yeast-mgll |
| Inhibitor | C18-octadecyl-MAG-like-phosphonate |
| Gene_locus | yeast-mgll |
| Family | Monoglyceridelipase_lysophospholip |
| Structure | 4ZXF 4ZWN |
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 Commun
71 :243
Rengachari S, Aschauer P, Sturm C, Oberer M (2015)
Acta Crystallographica F Struct Biol Commun
71 :243