Crystallization and preliminary X-ray crystallographic analysis of tyrosinase from the mushroom Agaricus bisporus

Tyrosinase catalyzes the conversion of tyrosine to dihydroxyphenylalanine quinone, which is the main precursor for the biosynthesis of melanin. The enzyme from Agaricus bisporus, the common button mushroom, was purified and crystallized in two different space groups. Crystals belonging to space group P2(1) (unit-cell parameters a = 104.2, b = 105.0, c = 119.1 angstrom, beta = 110.6 degrees, four molecules per asymmetric unit) diffracted to 3.0 angstrom resolution. Crystals belonging to space group P2(1)2(1)2 (unit-cell parameters a = 104.0, b = 104.5, c = 108.4 angstrom, two molecules per asymmetric unit) diffracted to 2.6 angstrom resolution. It was essential to include 5 mM HoCl3 in all crystallization conditions in order to obtain well diffracting crystals