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

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Stefan KernstockChristoph Mueller-Dieckmann

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 A.

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Citations

Oct 4, 2006·Proceedings of the National Academy of Sciences of the United States of America·Christoph Mueller-DieckmannFriedrich Koch-Nolte
Mar 8, 2008·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Christoph Mueller-DieckmannFriedrich Koch-Nolte
May 2, 2009·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Stefan KernstockChristoph Mueller-Dieckmann
May 19, 2007·Experimental Cell Research·Ralph G MeyerMyron K Jacobson
Jun 27, 2017·ELife·Pietro FontanaIvan Ahel

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