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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 3(62), p. 224-227, 2006

DOI: 10.1107/s1744309106003435

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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase

Journal article published in 2006 by Stefan Kernstock, Friedrich Koch-Nolte ORCID, Jochen Mueller-Dieckmann, Manfred S. Weiss, Christoph Mueller-Dieckmann
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This paper is available in a repository.

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Abstract

ADP-ribosylhydrolases catalyze the release of ADP-ribose from ADP-ribosylated proteins via hydrolysis of the glycosidic bond between ADP-ribose and a specific amino-acid residue in a target protein. Human ADP-ribosylhydrolase 3, consisting of 347 amino-acid residues, has been cloned and heterologously expressed in Escherichia coli, purified and crystallized in two different space groups. Preliminary X-ray diffraction studies yielded excellent diffraction data to a resolution of 1.6 Å. © 2006 International Union of Crystallography. All rights reserved.