title: Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase.
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.
authors.affiliation: Institut für Immunologie, Universitätsklinikum Eppendorf, D-20246 Hamburg, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Kernstock
authors.forename: Friedrich
authors.initials: F
authors.lastname: Koch-Nolte
authors.forename: Jochen
authors.initials: J
authors.lastname: Mueller-Dieckmann
authors.forename: Manfred S
authors.initials: MS
authors.lastname: Weiss
authors.forename: Christoph
authors.initials: C
authors.lastname: Mueller-Dieckmann
mesh_terms: D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans
chemical_list: D006026:Glycoside Hydrolases; C508145:ADPRS protein, human