Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 61; no. 10; pp. 942 - 944
• Main Authors: Wright, Helena, Kiss, András L., Szeltner, Zoltán, Polgár, László, Fülöp, Vilmos
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.10.2005; International Union of Crystallography
• Subjects: acylaminoacyl peptidase; Animals; ATOMS; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CROSS-LINKING; Cross-Linking Reagents - pharmacology; Cryopreservation; CRYSTALLIZATION; Crystallization Communications; Crystallography, X-Ray; CRYSTALS; DIFFUSION; EUROPEAN SYNCHROTRON RADIATION FACILITY; Hydrolysis; LIVER; Liver - metabolism; Models, Statistical; MOLECULES; Peptide Hydrolases - chemistry; Polyethylene Glycols - chemistry; porcine liver; Protein Structure, Tertiary; RESOLUTION; SPACE GROUPS; Swine; X-Ray Diffraction
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309105029222

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.