title: 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, 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 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.
authors.affiliation: Laboratory of Biophysical Chemistry, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
authors.forename: Wangsa T
authors.initials: WT
authors.lastname: Ismaya
authors.forename: Henriëtte J
authors.initials: HJ
authors.lastname: Rozeboom
authors.forename: Marloes
authors.initials: M
authors.lastname: Schurink
authors.forename: Carmen G
authors.initials: CG
authors.lastname: Boeriu
authors.forename: Harry
authors.initials: H
authors.lastname: Wichers
authors.forename: Bauke W
authors.initials: BW
authors.lastname: Dijkstra
mesh_terms: D000364:Agaricus / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D014442:Monophenol Monooxygenase / Q000737:chemistry*
chemical_list: D014442:Monophenol Monooxygenase