Open AccessCrystallization and preliminary X‐ray crystallographic analysis of β‐galactosidase from Kluyveromyces lactis
Author(s) -
PereiraRodríguez Ángel,
FernándezLeiro Rafael,
González Siso M. Isabel,
Cerdán M. Esperanza,
Becerra Manuel,
SanzAparicio Julia
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109054931
Subject(s) - kluyveromyces lactis , crystallization , lactose , yeast , protein crystallization , kluyveromyces , crystallography , x ray crystallography , crystal (programming language) , resolution (logic) , diffraction , chemistry , materials science , biochemistry , saccharomyces cerevisiae , organic chemistry , physics , optics , artificial intelligence , computer science , programming language
β‐Galactosidase from Kluyveromyces lactis catalyses the hydrolysis of the β‐galactosidic linkage in lactose. Owing to its many industrial applications, the biotechnological potential of this enzyme is substantial. This protein has been expressed in yeast and purified for crystallization trials. However, optimization of the best crystallization conditions yielded crystals with poor diffraction quality that precluded further structural studies. Finally, the crystal quality was improved using the streak‐seeding technique and a complete diffraction data set was collected at 2.8 Å resolution.