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Crystallization and preliminary X-ray diffraction analysis of the small laccase from Streptomyces coelicolor.

ABSTRACT: The small bacterial laccase from the actinobacterium Streptomyces coelicolor which lacks the second of the three domains of the laccases structurally characterized to date was crystallized. This multi-copper phenol oxidase crystallizes in a primitive tetragonal lattice, with unit-cell parameters a = b = 179.8, c = 175.3 A. The crystals belong to either space group P4(1)2(1)2 or P4(3)2(1)2. The self-rotation function shows the presence of a noncrystallographic threefold axis in the structure. Phases will be determined from the anomalous signal of the natively present copper ions.

SUBMITTER: Skalova T

PROVIDER: S-EPMC2344102 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of the small laccase from Streptomyces coelicolor.

Skálová Tereza T Dohnálek Jan J Ostergaard Lars Henrik LH Ostergaard Peter Rahbek PR Kolenko Petr P Dusková Jarmila J Hasek Jindrich J

Acta crystallographica. Section F, Structural biology and crystallization communications 20071130 Pt 12

The small bacterial laccase from the actinobacterium Streptomyces coelicolor which lacks the second of the three domains of the laccases structurally characterized to date was crystallized. This multi-copper phenol oxidase crystallizes in a primitive tetragonal lattice, with unit-cell parameters a = b = 179.8, c = 175.3 A. The crystals belong to either space group P4(1)2(1)2 or P4(3)2(1)2. The self-rotation function shows the presence of a noncrystallographic threefold axis in the structure. Pha ...[more]

PMID: 18084099

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