UNSPECIFIED. (2004) Expression, purification and preliminary crystallographic analysis of dipeptidyl peptidase IV from Porphyromonas gingivalis. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 60 (Part 10). pp. 1871-1873. ISSN 0907-4449

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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 Angstrom 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 Angstrom, beta = 95.0degrees. 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.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology
Journal or Publication Title:	ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
Publisher:	BLACKWELL MUNKSGAARD
ISSN:	0907-4449
Date:	October 2004
Volume:	60
Number:	Part 10
Number of Pages:	3
Page Range:	pp. 1871-1873
Identification Number:	10.1107/S0907444904017639
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/8012

Data sourced from Thomson Reuters' Web of Knowledge

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