Purification, crystallization and preliminary X‐ray diffraction analysis of a soluble variant of the monoglyceride lipase Yju3p from the yeast Saccharomyces cerevisiae. Issue 2 (1st February 2015)

• Record Type: Journal Article
• Authors: Rengachari, Srinivasan; Aschauer, Philipp; Sturm, Christian; Oberer, Monika
• Is Part Of: Acta crystallographica. Volume 71:Issue 2(2015:Feb.)
• Page Start: 243
• Page End: 246
• Publication Date: 2015-02-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X15001557
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The protein Yju3p is the orthologue of monoglyceride lipases in the yeast <italic>Saccharomyces cerevisiae</italic>. 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 <italic>P</italic>2₁2₁2₁), with unit‐cell parameters <italic>a</italic> = 77.2, <italic>b</italic> = 108.6, <italic>c</italic> = 167.7 Å. The asymmetric unit contained four molecules with a solvent content of 46.4%.</p> </abstract>