Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase
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 1744-3091Full text not available from this repository.
Official URL: http://dx.doi.org/10.1107/S1744309105029222
Acylaminoacyl peptidase (also known as acylamino-acid-releasing enzyme or acylpeptide hydrolase; EC 22.214.171.124) 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|
|Official Date:||October 2005|
|Number of Pages:||3|
|Page Range:||pp. 942-944|
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