Crystallization and X-ray diffraction studies of a two-domain laccase from Streptomyces griseoflavus

Acta Crystallographica. Section F, Structural Biology Communications
S V TishchenkoA A Leontievsky

Abstract

Laccase (EC 1.10.3.2) is one of the most common copper-containing oxidases; it is found in many organisms and catalyzes the oxidation of primarily phenolic compounds by oxygen. Two-domain laccases have unusual thermostability, resistance to inhibitors and an alkaline optimum of activity. The causes of these properties in two-domain laccases are poorly understood. A recombinant two-domain laccase (SgfSL) was cloned from the genome of Streptomyces griseoflavus Ac-993, expressed in Escherichia coli and purified to homogeneity. The crystals of SgfSL belonged to the monoclinic space group P21, with unit-cell parameters a = 74.64, b = 94.72, c = 117.40 Å, β = 90.672°, and diffraction data were collected to 2.0 Å resolution using a synchrotron-radiation source. Two functional trimers per asymmetric unit correspond to a Matthews coefficient of 1.99 Å(3) Da(-1) according to the monomer molecular weight of 35.6 kDa.

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Citations

Jul 3, 2019·International Journal of Molecular Sciences·Azat GabdulkhakovSvetlana Tishchenko
Sep 20, 2019·Journal of Inorganic Biochemistry·Anna C OlbrichVlada B Urlacher

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