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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology Communications, 2(71), p. 243-246, 2015

DOI: 10.1107/s2053230x15001557

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

Journal article published in 2015 by Srinivasan Rengachari, Philipp Aschauer, Christian Sturm, Monika Oberer ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The protein Yju3p is the orthologue of monoglyceride lipases in the yeastSaccharomyces 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 groupP212121), with unit-cell parametersa= 77.2,b= 108.6,c= 167.7 Å. The asymmetric unit contained four molecules with a solvent content of 46.4%.