title: 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.
authors.affiliation: Departamento de Bioloxía Celular e Molecular, Facultade de Ciencias, Universidade da Coruña, Campus da Zapateira s/n, 15071 A Coruña, Spain.
authors.forename: Angel
authors.initials: A
authors.lastname: Pereira-Rodríguez
authors.forename: Rafael
authors.initials: R
authors.lastname: Fernández-Leiro
authors.forename: M Isabel
authors.initials: MI
authors.lastname: González Siso
authors.forename: M Esperanza
authors.initials: ME
authors.lastname: Cerdán
authors.forename: Manuel
authors.initials: M
authors.lastname: Becerra
authors.forename: Julia
authors.initials: J
authors.lastname: Sanz-Aparicio
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D007716:Kluyveromyces / Q000201:enzymology*; D001616:beta-Galactosidase / Q000737:chemistry*
chemical_list: D001616:beta-Galactosidase