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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. doi:10.1107/S1744309105029222 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 | ||||
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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 F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS | ||||
Publisher: | BLACKWELL PUBLISHING | ||||
ISSN: | 1744-3091 | ||||
Official Date: | October 2005 | ||||
Dates: |
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Volume: | 61 | ||||
Number: | Part 10 | ||||
Number of Pages: | 3 | ||||
Page Range: | pp. 942-944 | ||||
DOI: | 10.1107/S1744309105029222 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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