biostudies-literatureUnknown66(Pt 9)Sendovski MTyrosinases are type 3 copper enzymes that are involved in the production of melanin and have two copper ions in the active site. Here, the crystallization and primary analysis of a tyrosinase from Bacillus megaterium is reported. The purified protein was crystallized in the absence or presence of zinc ions and the crystals diffracted to a resolution of 2.0 A. Crystals obtained in the presence of zinc belonged to space group P2(1)2(1)2(1), while crystals grown in the absence of zinc belonged to space group P2(1). In both space groups the asymmetric unit contained a dimer, with minor differences in the crystal density and in packing interactions.Acta crystallographica. Section F, Structural biology and crystallization communications1101-3https://www.ebi.ac.uk/biostudies/studies/S-EPMC2935238biostudies-literatureCrystallization and preliminary X-ray crystallographic analysis of a bacterial tyrosinase from Bacillus megaterium.PMC2935238Adir NFishman AShuster Ben-Yosef VKanteev MSendovski MfalseCrystallization and preliminary X-ray crystallographic analysis of a bacterial tyrosinase from Bacillus megaterium.Tyrosinases are type 3 copper enzymes that are involved in the production of melanin and have two copper ions in the active site. Here, the crystallization and primary analysis of a tyrosinase from Bacillus megaterium is reported. The purified protein was crystallized in the absence or presence of zinc ions and the crystals diffracted to a resolution of 2.0 A. Crystals obtained in the presence of zinc belonged to space group P2(1)2(1)2(1), while crystals grown in the absence of zinc belonged to space group P2(1). In both space groups the asymmetric unit contained a dimer, with minor differences in the crystal density and in packing interactions.2010-01-01T00:00:00Z2010 Sep2024-11-21T01:02:01.811Z2019-03-27T00:00:48ZS-EPMC29352382082353710.1107/s174430911003152010.1107/S1744309110031520