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Updated: Aug 11, 2026
Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit
Published on: June 28, 2013
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the
Stefan Kernstock1, Friedrich Koch-Nolte, Jochen Mueller-Dieckmann
1Institut für Immunologie, Universitätsklinikum Eppendorf, D-20246 Hamburg, Germany.
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.
