Back to Search Start Over

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

Authors :
Mueller-Dieckmann C
Scheuermann T
Wursthorn K
Schröder J
Haag F
Schulz GE
Koch-Nolte F
Source :
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2002 Jul; Vol. 58 (Pt 7), pp. 1211-3. Date of Electronic Publication: 2002 Jun 20.
Publication Year :
2002

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.

Details

Language :
English
ISSN :
0907-4449
Volume :
58
Issue :
Pt 7
Database :
MEDLINE
Journal :
Acta crystallographica. Section D, Biological crystallography
Publication Type :
Academic Journal
Accession number :
12077446
Full Text :
https://doi.org/10.1107/s090744490200700x