| Title : Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase - Wright_2005_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_61_942 |
| Author(s) : Wright H , Kiss AL , Szeltner Z , Polgar L , Fulop V |
| Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 61 :942 , 2005 |
| 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 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. |
| ESTHER : Wright_2005_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_61_942 |
| PubMedSearch : Wright_2005_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_61_942 |
| PubMedID: 16511202 |
| Gene_locus related to this paper: aerpe-APE1547 |
| Gene_locus related to this paper: aerpe-APE1547 |
Wright H, Kiss AL, Szeltner Z, Polgar L, Fulop V (2005)
Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase
Acta Crystallographica Sect F Struct Biol Cryst Commun
61 :942
Wright H, Kiss AL, Szeltner Z, Polgar L, Fulop V (2005)
Acta Crystallographica Sect F Struct Biol Cryst Commun
61 :942