Open AccessCrystallization and preliminary X‐ray crystallographic analysis of tyrosinase from the mushroom Agaricus bisporus
Author(s) -
Ismaya Wangsa T.,
Rozeboom Henriëtte J.,
Schurink Marloes,
Boeriu Carmen G.,
Wichers Harry,
Dijkstra Bauke W.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911100738x
Subject(s) - agaricus bisporus , crystallization , tyrosinase , agaricus , molecule , chemistry , space group , mushroom , x ray crystallography , crystallography , stereochemistry , resolution (logic) , diffraction , enzyme , biochemistry , organic chemistry , physics , food science , optics , artificial intelligence , computer science
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 P 2 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 P 2 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 m M HoCl 3 in all crystallization conditions in order to obtain well diffracting crystals.