Crystallization and X-ray diffraction studies of a two-domain laccase from Streptomyces griseoflavus

Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1200-4. doi: 10.1107/S2053230X15014375. Epub 2015 Aug 25.


Laccase (EC is one of the most common copper-containing oxidases; it is found in many organisms and catalyzes the oxidation of primarily phenolic compounds by oxygen. Two-domain laccases have unusual thermostability, resistance to inhibitors and an alkaline optimum of activity. The causes of these properties in two-domain laccases are poorly understood. A recombinant two-domain laccase (SgfSL) was cloned from the genome of Streptomyces griseoflavus Ac-993, expressed in Escherichia coli and purified to homogeneity. The crystals of SgfSL belonged to the monoclinic space group P21, with unit-cell parameters a = 74.64, b = 94.72, c = 117.40 Å, β = 90.672°, and diffraction data were collected to 2.0 Å resolution using a synchrotron-radiation source. Two functional trimers per asymmetric unit correspond to a Matthews coefficient of 1.99 Å(3) Da(-1) according to the monomer molecular weight of 35.6 kDa.

Keywords: Streptomyces griseoflavus; two-domain laccase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallization
  • Laccase / chemistry*
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Spectrophotometry, Ultraviolet
  • Static Electricity
  • Streptomyces / enzymology*
  • X-Ray Diffraction


  • Laccase