Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase.
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 A 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 A and four molecules in the asymmetric unit.
Wright
Helena
H
Department of Biological Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, England.
Kiss
András L
AL
Szeltner
Zoltán
Z
Polgár
László
L
Fülöp
Vilmos
V
D000818:Animals; D003432:Cross-Linking Reagents / Q000494:pharmacology; D015925:Cryopreservation; D003460:Crystallization; D018360:Crystallography, X-Ray; D006868:Hydrolysis; D008099:Liver / Q000378:metabolism; D015233:Models, Statistical; D010447:Peptide Hydrolases / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry; D017434:Protein Structure, Tertiary; D013552:Swine; D014961:X-Ray Diffraction
D003432:Cross-Linking Reagents; D011092:Polyethylene Glycols; D010447:Peptide Hydrolases; C028759:oligopeptidase; C038220:acylaminoacyl-peptidase