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Expression, purification, crystallization and preliminary X-ray analysis of rat ecto-ADP-ribosyltransferase 2 (ART2.2) by Christoph Mueller-Dieckmann; Till Scheuermann; Karsten Wursthorn; Jens Schröder; Friedrich Haag; Georg E. Schulz; Friedrich Koch-Nolte is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Expression, purification, crystallization and preliminary X-ray analysis of rat ecto-ADP-ribosyltransferase 2 (ART2.2) about?

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.

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Author

Christoph Mueller-Dieckmann; Till Scheuermann; Karsten Wursthorn; Jens Schröder; Friedrich Haag; Georg E. Schulz; Friedrich Koch-Nolte

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

2002

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)