Crystallization and X-ray diffraction analysis of a catalytic domain of hyperthermophilic chitinase from Pyrococcus furiosus

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt 8):791-3. doi: 10.1107/S1744309106026157. Epub 2006 Jul 25.

Abstract

The crystallization and preliminary X-ray diffraction analysis of a catalytic domain of chitinase (PF1233 gene) from the hyperthermophilic archaeon Pyrococcus furiosus is reported. The recombinant protein, prepared using an Escherichia coli expression system, was crystallized by the hanging-drop vapour-diffusion method. An X-ray diffraction data set was collected at the undulator beamline BL44XU at SPring-8 to a resolution of 1.50 angstroms. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 90.0, b = 92.8, c = 107.2 angstroms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Archaeal Proteins / chemistry
  • Archaeal Proteins / isolation & purification
  • Archaeal Proteins / metabolism
  • Catalytic Domain
  • Chitinases / chemistry*
  • Chitinases / isolation & purification
  • Chitinases / metabolism
  • Cloning, Molecular
  • Crystallization
  • Escherichia coli / enzymology
  • Molecular Sequence Data
  • Pyrococcus furiosus / enzymology*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Thermodynamics
  • X-Ray Diffraction

Substances

  • Archaeal Proteins
  • Recombinant Proteins
  • Chitinases