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Crystallization and preliminary X-ray diffraction analysis of the small laccase from Streptomyces coelicolor
T Skalova, J Dohnalek, LH Ostergaard, PR Ostergaard, P Kolenko, J Duskova, J Hasek
Jazyk angličtina Země Velká Británie
NLK
Free Medical Journals
od 2005 do 2013
PubMed Central
od 2005 do 2013
Europe PubMed Central
od 2005 do 2013
Medline Complete (EBSCOhost)
od 2005-01-01 do 2007-12-31
Wiley Online Library (archiv)
od 2005-01-01 do 2012-12-31
- MeSH
- difrakce rentgenového záření MeSH
- financování organizované MeSH
- krystalizace MeSH
- lakasa genetika chemie metabolismus MeSH
- molekulová hmotnost MeSH
- Streptomyces coelicolor enzymologie genetika 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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- $a Institute of Macromolecular Chemistry, Academy of Sciences of the Czech Republic, Heyrovskeho nam. 2, 162 06 Praha 6, Czech Republic. skalova@imc.cas.cz
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- $a 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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