Rea_2004_Acta.Crystallogr.D.Biol.Crystallogr_60_1871

Reference

Title : Expression, purification and preliminary crystallographic analysis of dipeptidyl peptidase IV from Porphyromonas gingivalis - Rea_2004_Acta.Crystallogr.D.Biol.Crystallogr_60_1871
Author(s) : Rea D , Lambeir AM , Kumagai Y , De Meester I , Scharpe S , Fulop V
Ref : Acta Crystallographica D Biol Crystallogr , 60 :1871 , 2004
Abstract :

The asaccharolytic periodontopathogen Porphyromonas gingivalis produces membrane-anchored proteases such as dipeptidyl peptidase IV that are involved in the destruction of host periodontal tissue. The extracellular domain of this enzyme was overexpressed in Escherichia coli as an N-terminal His-tag fusion protein, purified using standard metal-affinity chromatography and crystallized using the hanging-drop vapour-diffusion technique in 40% 2-methyl-2,4-pentanediol and 100 mM Tris-HCl pH 8.0. Diffraction data to 2.7 A resolution were collected using synchrotron radiation. The crystals belong to space group P2(1), with unit-cell parameters a = 117.0, b = 112.9, c = 310.0 A, beta = 95.0 degrees. There are ten molecules per asymmetric unit, indicating a solvent content of 50%. Data were also collected from selenomethionine-derived crystals and structure solution by SAD or MAD is in progress.

PubMedSearch : Rea_2004_Acta.Crystallogr.D.Biol.Crystallogr_60_1871
PubMedID: 15388936
Gene_locus related to this paper: porgi-DPP

Related information

Gene_locus porgi-DPP
Family porgi-DPP    DPP4N_Peptidase_S9

Citations formats

Rea D, Lambeir AM, Kumagai Y, De Meester I, Scharpe S, Fulop V (2004)
Expression, purification and preliminary crystallographic analysis of dipeptidyl peptidase IV from Porphyromonas gingivalis
Acta Crystallographica D Biol Crystallogr 60 :1871

Rea D, Lambeir AM, Kumagai Y, De Meester I, Scharpe S, Fulop V (2004)
Acta Crystallographica D Biol Crystallogr 60 :1871