Purification and preliminary crystallographic study of Trametes versicolor laccase in its native form
Related Experiment Video
Updated: Oct 2, 2026

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method
Published on: July 27, 2016
Thomas Bertrand1, Claude Jolivalt, Eliane Caminade
1Laboratoire d'Enzymologie et de Biochimie Structurales, UPR 9063 du CNRS, 91198 Gif-sur-Yvette CEDEX, France.
Abstract:
Laccases are multi-copper oxidases that catalyse the oxidation of a wide range of phenols and their use in industrial oxidative processes is increasing. A laccase has been purified from the fungus Trametes versicolor and crystallized using the hanging-drop method. Crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 87.7, b = 110.5, c = 123.2 A, beta = 103.4 degrees. A complete data set was collected to 2.4 A resolution on a Cu K(alpha) rotating-anode X-ray source. Molecular replacement was performed and the initial electron-density maps indicate that the four expected Cu atoms are all present.
