Crystallization and preliminary X-ray diffraction analysis of the small laccase from Streptomyces coelicolor
Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
18084099
PubMed Central
PMC2344102
DOI
10.1107/s1744309107060721
PII: S1744309107060721
Knihovny.cz E-zdroje
- MeSH
- difrakce rentgenového záření MeSH
- krystalizace MeSH
- lakasa chemie genetika metabolismus MeSH
- molekulová hmotnost MeSH
- Streptomyces coelicolor enzymologie genetika MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- lakasa MeSH
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.
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