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Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase
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UNSPECIFIED. (2005) Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 61 (Part 10). pp. 942-944. ISSN 1744-3091
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Official URL: http://dx.doi.org/10.1107/S1744309105029222
Abstract
Acylaminoacyl peptidase (also known as acylamino-acid-releasing enzyme or acylpeptide hydrolase; EC 3.4.19.1) is an unusual member of the prolyl oligopeptidase family catalysing the hydrolysis of an N-acylated peptide to an acylamino acid and a peptide with a free N-terminus. Acylaminoacyl peptidase purified from porcine liver has been crystallized in mother liquor containing 0.1 M Tris-HCl pH 7.0, 10%(w/v) polyethylene glycol 8000, 50 mM MgCl2 and 1%(w/v) CHAPS using the hanging-drop vapour-diffusion technique. A full data set to 3.4 angstrom resolution was collected at ESRF beamline ID14-4 and space group C222 was assigned, with unit-cell parameters a = 84.8, b = 421.1, c = 212.0 angstrom and four molecules in the asymmetric unit.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
| Journal or Publication Title: | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS |
| Publisher: | BLACKWELL PUBLISHING |
| ISSN: | 1744-3091 |
| Date: | October 2005 |
| Volume: | 61 |
| Number: | Part 10 |
| Number of Pages: | 3 |
| Page Range: | pp. 942-944 |
| Identification Number: | 10.1107/S1744309105029222 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/34516 |
Data sourced from Thomson Reuters' Web of Knowledge
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