Crystallization and preliminary X-ray diffraction study of an active-site mutant of pro-Tk-subtilisin from a hyperthermophilic archaeon

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt 9):902-5. doi: 10.1107/S1744309106030454. Epub 2006 Aug 18.

Abstract

Crystallization of and preliminary crystallographic studies on an active-site mutant of pro-Tk-subtilisin from the hyperthermophilic archaeon Thermococcus kodakaraensis were performed. The crystal was grown at 277 K by the sitting-drop vapour-diffusion method. Native X-ray diffraction data were collected to 2.3 A resolution using synchrotron radiation from station BL41XU at SPring-8. The crystal belongs to the orthorhombic space group I222, with unit-cell parameters a = 92.69, b = 121.78, c = 77.53 A. Assuming the presence of one molecule per asymmetric unit, the Matthews coefficient V(M) was calculated to be 2.6 A(3) Da(-1) and the solvent content was 53.1%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / genetics*
  • Binding Sites / genetics
  • Crystallization
  • Enzyme Precursors / chemistry*
  • Enzyme Precursors / genetics*
  • Enzyme Precursors / metabolism
  • Mutation*
  • Peptide Fragments / chemistry*
  • Peptide Fragments / genetics*
  • Peptide Fragments / metabolism
  • Subtilisins / chemistry*
  • Subtilisins / genetics*
  • Subtilisins / metabolism
  • Thermococcus / chemistry*
  • Thermococcus / genetics*
  • X-Ray Diffraction / methods

Substances

  • Archaeal Proteins
  • Enzyme Precursors
  • Peptide Fragments
  • prosubtilisin
  • Subtilisins