Literature DB >> 18084099

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

Tereza Skálová1, Jan Dohnálek, Lars Henrik Ostergaard, Peter Rahbek Ostergaard, Petr Kolenko, Jarmila Dusková, Jindrich Hasek.   

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.

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Year:  2007        PMID: 18084099      PMCID: PMC2344102          DOI: 10.1107/S1744309107060721

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  11 in total

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  5 in total

1.  Structure of laccase from Streptomyces coelicolor after soaking with potassium hexacyanoferrate and at an improved resolution of 2.3 Å.

Authors:  Tereza Skálová; Jarmila Dušková; Jindřich Hašek; Andrea Stěpánková; Tomáš Koval; Lars Henrik Østergaard; Jan Dohnálek
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2010-12-21

2.  Purification, crystallization and preliminary X-ray structure analysis of the laccase from Ganoderma lucidum.

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Review 4.  Functional and protective hole hopping in metalloenzymes.

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5.  Laccase SilA from Streptomyces ipomoeae CECT 3341, a key enzyme for the degradation of lignin from agricultural residues?

Authors:  Alba Blánquez; Andrew S Ball; José Antonio González-Pérez; Nicasio T Jiménez-Morillo; Francisco González-Vila; M Enriqueta Arias; Manuel Hernández
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  5 in total

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