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

W.T. Ismaya, H.J. Rozeboom, M. Schurink, C.G. Boeriu, H.J. Wichers, B.W. Dijkstra

Research output: Contribution to journalArticleAcademicpeer-review

28 Citations (Scopus)

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 P21 (unit-cell parameters a = 104.2, b = 105.0, c = 119.1 Å, ß = 110.6°, four molecules per asymmetric unit) diffracted to 3.0 Å resolution. Crystals belonging to space group P21212 (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 HoCl3 in all crystallization conditions in order to obtain well diffracting crystals.
Original languageEnglish
Pages (from-to)575-578
JournalActa Crystallographica Section F. Structural Biology and Crystallization Communications
Volume67
Issue number5
DOIs
Publication statusPublished - 2011

Keywords

  • diphenolase activities
  • polyphenol oxidase
  • monophenolase
  • expression
  • mechanism

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