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Expression, purification, crystallization and preliminary X-ray analysis of rat ecto-ADP-ribosyltransferase 2 (ART2.2).
- 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.
- Subjects :
- ADP Ribose Transferases metabolism
Animals
Antigens, Differentiation, T-Lymphocyte
Cell Line
Cricetinae
Escherichia coli metabolism
Humans
Hydrogen-Ion Concentration
Insecta
Membrane Glycoproteins metabolism
Periplasm metabolism
Plasmids metabolism
Rats
Temperature
Time Factors
ADP Ribose Transferases chemistry
Crystallography, X-Ray methods
Membrane Glycoproteins chemistry
Subjects
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