Crystallization and preliminary X-ray analysis of carboxypeptidase 1 from Thermus thermophilus

Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1445-6. doi: 10.1107/S0907444904012557. Epub 2004 Jul 21.

Abstract

Carboxypeptidase 1 from the thermophilic eubacterium Thermus thermophilus (TthCP1, 58 kDa), a member of the M32 family of metallocarboxypeptidases, was crystallized by the sitting-drop vapour-diffusion method using PEG 8000 as the precipitant. The crystals diffracted X-rays to beyond 2.6 A resolution using a synchrotron-radiation source. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 171.0, b = 231.6, c = 124.9 A. The crystal contains three molecules in an asymmetric unit (VM = 2.11 A3 Da(-1)) and has a solvent content of 61.5%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carboxypeptidases / chemistry*
  • Carboxypeptidases / genetics
  • Carboxypeptidases / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Spectrometry, Fluorescence
  • Thermus thermophilus / enzymology*
  • Thermus thermophilus / genetics

Substances

  • Carboxypeptidases