Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase

Helena Wright, András L. Kiss, Z. Szeltner, L. Polgár, Vilmos Fülöp

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Acylaminoacyl peptidase (also known as acylamino-acid-releasing enzyme or acylpeptide hydrolase; EC 3.4.19.1) is an unusual member of the prolyl oligopeptidase family catalysing the hydrolysis of an N-acylated peptide to an acylamino acid and a peptide with a free N-terminus. Acylaminoacyl peptidase purified from porcine liver has been crystallized in mother liquor containing 0.1 M Tris-HCl pH 7.0, 10%(w/v) polyethylene glycol 8000, 50 mM MgCl2 and 1%(w/v) CHAPS using the hanging-drop vapour-diffusion technique. A full data set to 3.4 Å resolution was collected at ESRF beamline ID14-4 and space group C222 was assigned, with unit-cell parameters a = 84.8, b = 421.1, c = 212.0 Å and four molecules in the asymmetric unit.

Original languageEnglish
Pages (from-to)942-944
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number10
DOIs
Publication statusPublished - 2005

Fingerprint

Crystallization
peptides
Swine
crystallization
acids
releasing
liver
prolyl oligopeptidase
hydrolysis
enzymes
glycols
polyethylenes
vapors
Peptides
Magnesium Chloride
cells
Liver
molecules
Hydrolysis
Vapors

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase. / Wright, Helena; Kiss, András L.; Szeltner, Z.; Polgár, L.; Fülöp, Vilmos.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 61, No. 10, 2005, p. 942-944.

Research output: Contribution to journalArticle

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