Characterization and crystallization of active domains of a novel luciferase from a marine dinoflagellate

Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):761-4. doi: 10.1107/s0907444903002920. Epub 2003 Mar 25.

Abstract

Lingulodinium polyedrum luciferase is a bioluminescent protein found in the marine dinoflagellate formerly known as Gonyaulax. It is located in organelles called scintillons that emit brief and bright flashes of light that are regulated by an endogenous circadian clock. The complete luciferase molecule has a molecular mass of 136 994 Da and contains three homologous domains, each of which is a separately active luciferase. Two of these domains, D2-LCF and D3-LCF, have been cloned, expressed and crystallized. Crystals of D2-LCF were obtained from PEG 10 000 in space group P2(1)2(1)2(1), with unit-cell parameters a = 49.1, b = 104.7, c = 180.3 A. They diffract to 2.9 A on a rotating anode. Crystals of D3-LCF were grown from PEG 2000 in space group P2(1)2(1)2(1), with unit-cell parameters a = 58.86, b = 63.98, c = 95.76 A. They diffract to 2.3 A on a rotating anode.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Binding Sites
  • Cloning, Molecular
  • Crystallization
  • Dinoflagellida / enzymology*
  • Dinoflagellida / genetics
  • Dinoflagellida / ultrastructure
  • Gene Expression
  • Hydrogen-Ion Concentration
  • Indicators and Reagents
  • Luciferases / chemistry*
  • Luciferases / genetics
  • Selenomethionine / chemistry
  • X-Ray Diffraction

Substances

  • Indicators and Reagents
  • Selenomethionine
  • Luciferases