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Expression, purification and preliminary crystallographic analysis of dipeptidyl peptidase IV from Porphyromonas gingivalis
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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. doi:10.1107/S0907444904017639 ISSN 0907-4449.
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Official URL: http://dx.doi.org/10.1107/S0907444904017639
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 | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
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Journal or Publication Title: | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | ||||
Publisher: | BLACKWELL MUNKSGAARD | ||||
ISSN: | 0907-4449 | ||||
Official Date: | October 2004 | ||||
Dates: |
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Volume: | 60 | ||||
Number: | Part 10 | ||||
Number of Pages: | 3 | ||||
Page Range: | pp. 1871-1873 | ||||
DOI: | 10.1107/S0907444904017639 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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