We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Crystallization and preliminary X-ray crystallographic analysis of latent isoform PPO4 mushroom ( Agaricus bisporus) tyrosinase.
- Authors
Mauracher, Stephan Gerhard; Molitor, Christian; Al-Oweini, Rami; Kortz, Ulrich; Rompel, Annette
- Abstract
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 Na6[TeW6O24]·22H2O as a co-crystallization agent.
- Subjects
CULTIVATED mushroom; PHENOL oxidase; X-ray crystallography; CRYSTALLIZATION; PHENOLS
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2014, Vol 70, Issue 2, p263
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X14000582