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Short Communication
Crystallization and preliminary X-ray investigation of a recombinant form of rat catechol O-methyltransferase
Article first published online: 3 FEB 2004
DOI: 10.1002/prot.340110309
Copyright © 1991 Wiley-Liss, Inc.
Issue
1097-0134/asset/cover.gif?v=1&s=d817e79b67ba6cacf8bdcce1a819c04de300a7e3 "Proteins: Structure, Function, and Bioinformatics")
Proteins: Structure, Function, and Bioinformatics
Volume 11, Issue 3, pages 233–236, November 1991
Additional Information
How to Cite
Vidgren, J., Tilgmann, C., Lundström, K. and Liljas, A. (1991), Crystallization and preliminary X-ray investigation of a recombinant form of rat catechol O-methyltransferase. Proteins, 11: 233–236. doi: 10.1002/prot.340110309
Publication History
- Issue published online: 3 FEB 2004
- Article first published online: 3 FEB 2004
- Manuscript Accepted: 29 APR 1991
- Abstract
- References
- Cited By
Keywords:
- protein crystals;
- X-ray crystallography;
- catechol O-methyltransferase;
- protein structure
Abstract
Rat catechol O-methyltransferase cDNA was introduced into an E. coli expression vector pKEX14, which utilizes the inducible T7 promoter. Active and soluble recombinant catechol O-methyltransferase was produced in bacteria and purified to electrophoretic homogeneity by chromatographic procedures. The purified enzyme has been crystallized by the method of vapor diffusion using polyethylene glycol as precipitant. The space group is P3121 or P3221 with a = b = 51.3 Å and c = 168.5 Å and one molecule in the asymmetric unit. The crystals diffract beyond 3.2 Å and are suitable for three-dimensional X-ray structure determination.