Crystallization and preliminary crystallographic analysis of acylamino-acid releasing enzyme from the hyperthermophilic archaeon Aeropyrum pernix

Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1054-5. doi: 10.1107/s0907444902005875. Epub 2002 May 29.

Abstract

Crystals of acylamino-acid releasing enzyme from the hyperthermophilic archaeon Aeropyrum pernix strain K1 have been grown at 291 K using ammonium phosphate as a precipitant. The diffraction pattern of the crystal extends to 2.4 A resolution at 100 K using Cu Kalpha radiation. The crystal belongs to space group P1, with unit-cell parameters a = 107.5, b = 109.9, c = 119.4 A, alpha = 108.1, beta = 109.8, gamma = 91.9 degrees. The presence of eight molecules per asymmetric unit gives a crystal volume per protein mass (V(M)) of 2.4 A(3) Da(-1) and a solvent content of 48% by volume. A full set of X-ray diffraction data was collected to 2.9 A from the native crystal.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaeal Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Desulfurococcaceae / enzymology*
  • Peptide Hydrolases / chemistry*
  • Protein Conformation

Substances

  • Archaeal Proteins
  • Peptide Hydrolases
  • acylaminoacyl-peptidase