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

ABSTRACT: 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 Å, ? = 110.6°, four molecules per asymmetric unit) diffracted to 3.0 Å resolution. Crystals belonging to space group P2(1)2(1)2 (unit-cell parameters a = 104.0, b = 104.5, c = 108.4 Å, two molecules per asymmetric unit) diffracted to 2.6 Å resolution. It was essential to include 5 mM HoCl(3) in all crystallization conditions in order to obtain well diffracting crystals.

SUBMITTER: Ismaya WT

PROVIDER: S-EPMC3087644 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature

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

Ismaya Wangsa T WT Rozeboom Henriëtte J HJ Schurink Marloes M Boeriu Carmen G CG Wichers Harry H Dijkstra Bauke W BW

Acta crystallographica. Section F, Structural biology and crystallization communications 20110427 Pt 5

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 Å, β = 110.6°, four molecules per asymmetric unit) diffracted to 3.0 Å resolution. Crystals belonging to space group P2(1)2(1)2 (unit-cell ...[more]

PMID: 21543865

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