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Structure of laccase from Streptomyces coelicolor after soaking with potassium hexacyanoferrate and at an improved resolution of 2.3 Å
T. Skálová, J. Dušková, J. Hašek, A. Stěpánková, T. Koval, LH. Østergaard, J. Dohnálek
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 2005 do 2013
PubMed Central
od 2005 do 2013
Europe PubMed Central
od 2005 do 2013
Wiley Online Library (archiv)
od 2005-01-01 do 2012-12-31
- MeSH
- bakteriální proteiny chemie MeSH
- barva MeSH
- ferrikyanidy chemie MeSH
- konformace proteinů MeSH
- krystalografie rentgenová MeSH
- lakasa chemie MeSH
- měď chemie MeSH
- molekulární modely MeSH
- molekulární sekvence - údaje MeSH
- stabilita enzymů MeSH
- Streptomyces coelicolor enzymologie MeSH
- vazebná místa MeSH
- železo chemie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
The paper reports the structure of the small laccase from Streptomyces coelicolor determined from a crystal soaked with potassium hexacyanoferrate [K4Fe(CN)6]. The decolorization of the natively blue crystal observed upon soaking indicates the reduction of the enzyme in the crystal. The ligand binds between laccase molecules and stabilizes the crystal. The increased diffraction limit of the diffraction data collected from this crystal enabled the refinement of the small laccase structure at 2.3 Å resolution, which is the highest resolution obtained to date.
Institute of Macromolecular Chemistry AS CR v v i Heyrovského nám 2 162 06 Praha 6 Czech Republic
Institute of Physics AS CR v v i Na Slovance 2 182 21 Praha 8 Czech Republic
Citace poskytuje Crossref.org
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