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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
Language English Country Great Britain
NLK
Free Medical Journals
from 2005 to 2013
PubMed Central
from 2005 to 2013
Europe PubMed Central
from 2005 to 2013
Medline Complete (EBSCOhost)
from 2005-01-01 to 2007-12-31
Wiley Online Library (archiv)
from 2005-01-01 to 2012-12-31
- MeSH
- X-Ray Diffraction MeSH
- Financing, Organized MeSH
- Crystallization MeSH
- Laccase genetics chemistry metabolism MeSH
- Molecular Weight MeSH
- Streptomyces coelicolor enzymology genetics 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.
References provided by Crossref.org
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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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