Open AccessCrystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase
Author(s) -
Wright Helena,
Kiss András L.,
Szeltner Zoltán,
Polgár László,
Fülöp Vilmos
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105029222
Subject(s) - crystallization , crystallography , materials science , chemistry , organic chemistry
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 m M MgCl 2 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 C 222 was assigned, with unit‐cell parameters a = 84.8, b = 421.1, c = 212.0 Å and four molecules in the asymmetric unit.