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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt 5):575-8. doi: 10.1107/S174430911100738X. Epub 2011 Apr 27.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agaricus / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Enzyme Stability
  • Monophenol Monooxygenase / chemistry*

Substances

  • Monophenol Monooxygenase