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Crystallization and preliminary X-ray crystallographic analysis of latent isoform PPO4 mushroom (Agaricus bisporus) tyrosinase

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      Polyphenol oxidase 4 (PPO4) from the natural source A. bisporus was crystallized in its latent precursor form (pro-tyrosinase; Ser2–Thr565) using the 6-tungstotellurate(VI) salt Na 6[TeW 6O 24]·22H 2O as a crystallization additive.


      Tyrosinase exhibits catalytic activity for the ortho-hydroxylation of monophenols to diphenols as well as their subsequent oxidation to quinones. Owing to polymerization of these quinones, brown-coloured high-molecular-weight compounds called melanins are generated. The latent precursor form of polyphenol oxidase 4, one of the six tyrosinase isoforms from Agaricus bisporus, was purified to homogeneity and crystallized. The obtained crystals belonged to space group C121 (two molecules per asymmetric unit) and diffracted to 2.78 Å resolution. The protein only formed crystals under low-salt conditions using the 6-tungstotellurate(VI) salt Na 6[TeW 6O 24]·22H 2O as a co-crystallization agent.

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      Author and article information

      [a ]Institut für Biophysikalische Chemie, Universität Wien , Althanstrasse 14, 1090 Wien, Austria
      [b ]School of Engineering and Science, Jacobs University , PO Box 750 561, 28759 Bremen, Germany
      Author notes
      Acta Crystallogr F Struct Biol Commun
      Acta Crystallogr F Struct Biol Commun
      Acta Cryst. F
      Acta Crystallographica. Section F, Structural Biology Communications
      International Union of Crystallography
      1 February 2014
      23 January 2014
      23 January 2014
      : 70
      : Pt 2 ( publisher-idID: f140200 )
      : 263-266
      ACSFEN S2053230X14000582
      © Mauracher et al. 2014

      This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.

      Crystallization Communications


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