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Expression, purification and preliminary crystallographic analysis of dipeptidyl peptidase IV from Porphyromonas gingivalis.
Acta Crystallogr D Biol Crystallogr. 2004 Oct; 60(Pt 10):1871-3.AC

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.

Authors+Show Affiliations

Rea D
Department of Biological Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, England.
Lambeir AM
No affiliation info available
Kumagai Y
No affiliation info available
De Meester I
No affiliation info available
Scharpé S
No affiliation info available
Fülöp V
No affiliation info available

MeSH

ChromatographyCloning, MolecularCrystallizationCrystallography, X-RayDipeptidyl Peptidase 4Escherichia coliPlasmidsPorphyromonas gingivalisRecombinant Fusion ProteinsSelenomethionineSynchrotronsX-Ray Diffraction

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15388936

Citation

Rea, Dean, et al. "Expression, Purification and Preliminary Crystallographic Analysis of Dipeptidyl Peptidase IV From Porphyromonas Gingivalis." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 10, 2004, pp. 1871-3.
Rea D, Lambeir AM, Kumagai Y, et al. Expression, purification and preliminary crystallographic analysis of dipeptidyl peptidase IV from Porphyromonas gingivalis. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 10):1871-3.
Rea, D., Lambeir, A. M., Kumagai, Y., De Meester, I., Scharpé, S., & Fülöp, V. (2004). Expression, purification and preliminary crystallographic analysis of dipeptidyl peptidase IV from Porphyromonas gingivalis. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 10), 1871-3.
Rea D, et al. Expression, Purification and Preliminary Crystallographic Analysis of Dipeptidyl Peptidase IV From Porphyromonas Gingivalis. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 10):1871-3. PubMed PMID: 15388936.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Expression, purification and preliminary crystallographic analysis of dipeptidyl peptidase IV from Porphyromonas gingivalis. AU - Rea,Dean, AU - Lambeir,Anne Marie, AU - Kumagai,Yumi, AU - De Meester,Ingrid, AU - Scharpé,Simon, AU - Fülöp,Vilmos, Y1 - 2004/09/23/ PY - 2004/06/01/received PY - 2004/07/17/accepted PY - 2004/9/25/pubmed PY - 2005/3/30/medline PY - 2004/9/25/entrez SP - 1871 EP - 3 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 10 N2 - 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. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15388936/Expression_purification_and_preliminary_crystallographic_analysis_of_dipeptidyl_peptidase_IV_from_Porphyromonas_gingivalis_ DB - PRIME DP - Unbound Medicine ER -