Title : Expression, purification and crystallization of human prolylcarboxypeptidase. - Abeywickrema_2010_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_66_702 |
Author(s) : Abeywickrema PD , Patel SB , Byrne NJ , Diehl RE , Hall DL , Ford RE , Rickert KW , Reid JC , Shipman JM , Geissler WM , Pryor KD , SinhaRoy R , Soisson SM , Lumb KJ , Sharma S |
Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 66 :702 , 2010 |
Abstract :
Prolylcarboxypeptidase (PrCP) is a lysosomal serine carboxypeptidase that cleaves a variety of C-terminal amino acids adjacent to proline and has been implicated in diseases such as hypertension and obesity. Here, the robust production, purification and crystallization of glycosylated human PrCP from stably transformed CHO cells is described. Purified PrCP yielded crystals belonging to space group R32, with unit-cell parameters a = b = 181.14, c = 240.13 A, that diffracted to better than 2.8 A resolution. |
PubMedSearch : Abeywickrema_2010_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_66_702 |
PubMedID: 20516604 |
Gene_locus related to this paper: human-PRCP |
Gene_locus | human-PRCP |
Structure | 3N2Z |
Abeywickrema PD, Patel SB, Byrne NJ, Diehl RE, Hall DL, Ford RE, Rickert KW, Reid JC, Shipman JM, Geissler WM, Pryor KD, SinhaRoy R, Soisson SM, Lumb KJ, Sharma S (2010)
Expression, purification and crystallization of human prolylcarboxypeptidase.
Acta Crystallographica Sect F Struct Biol Cryst Commun
66 :702
Abeywickrema PD, Patel SB, Byrne NJ, Diehl RE, Hall DL, Ford RE, Rickert KW, Reid JC, Shipman JM, Geissler WM, Pryor KD, SinhaRoy R, Soisson SM, Lumb KJ, Sharma S (2010)
Acta Crystallographica Sect F Struct Biol Cryst Commun
66 :702