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Crystallization and preliminary X-ray crystallographic analysis of beta-galactosidase from Kluyveromyces lactis.

ABSTRACT: Beta-galactosidase from Kluyveromyces lactis catalyses the hydrolysis of the beta-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 A resolution.

SUBMITTER: Pereira-Rodriguez A

PROVIDER: S-EPMC2833041 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic analysis of beta-galactosidase from Kluyveromyces lactis.

Pereira-Rodríguez Angel A Fernández-Leiro Rafael R González Siso M Isabel MI Cerdán M Esperanza ME Becerra Manuel M Sanz-Aparicio Julia J

Acta crystallographica. Section F, Structural biology and crystallization communications 20100224 Pt 3

Beta-galactosidase from Kluyveromyces lactis catalyses the hydrolysis of the beta-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 ...[more]

PMID: 20208165

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