Abstract
Kluyveromyces lactis β-galactosidase is an enzyme with numerous applications in the environmental, food and biotechnological industries. Despite of its biotechnological interest, its three-dimensional structure has not yet been determined. The growth of suitable crystals is an essential step in the structure determination of a protein by X-ray crystallography. At present, crystals are mostly grown using trial-and-error procedures since their growth often depends on the combination of many different factors. Testing the influence on crystallization of even only a small number of these factors requires many experimental set-ups and large amounts of protein. In the present work, a full-factorial design has been used in order to find conditions for obtaining good-quality crystals of K. lactis β-galactosidase. With this full-factorial method protein crystals have been obtained.
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