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Expression, purification, crystallization and preliminary X-ray analysis of rat ecto-ADP-ribosyltransferase 2
Christoph Mueller-Dieckmann1, Till Scheuermann, Karsten Wursthorn
1Institut für Organische Chemie und Biochemie, Albertstrasse 21, Freiburg im Breisgau 79104, Germany.
Abstract:
ADP-ribosyltransferases catalyze the transfer of the ADP-ribose moiety from NAD(+) onto proteins and other targets. These enzymes have been found in prokaryotes and in vertebrates; a eukaryotic enzyme structure is not yet known. The enzyme from Rattus norvegicus was expressed in the Escherichia coli periplasm at a level of about 0.2 mg per litre of culture, purified and crystallized. Native data sets were collected to 2.0 A resolution. A self-rotation function revealed a local twofold axis in crystal form A and a Patterson function showed a translational relationship in form B. Form C contains only one molecule in the asymmetric unit.