Schwede, T. F. and Badeker, M. and Langer, M. and Retey, J. and Schulz, G. E.. (1999) Homogenization and Crystallization of Histidine Ammonia-Lyase by Exchange of a Surface Cysteine Residue. Protein Engineering, 12 (2). pp. 151-153.
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Abstract
Histidase (histidine ammonia-lyase, EC 4.3.1.3) from Pseudomonas putida was expressed in Escherichia coli and purified. In the absence of thiols the tetrameric enzyme gave rise to undefined aggregates and suitable crystals could not be obtained. The solvent accessibility along the chain was predicted from the amino acid sequence. Among the seven cysteines, only one was labeled as 'solvent-exposed'. The exchange of this cysteine to alanine abolished all undefined aggregations and yielded readily crystals diffracting to 1.8 A resolution.
| Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum > Computational & Systems Biology > Bioinformatics (Schwede) |
|---|---|
| UniBasel Contributors: | Schwede, Torsten |
| Item Type: | Article, refereed |
| Article Subtype: | Research Article |
| Publisher: | Oxford University Press |
| ISSN: | 0269-2139 |
| e-ISSN: | 1460-213X |
| Note: | Publication type according to Uni Basel Research Database: Journal article |
| Identification Number: | |
| Last Modified: | 22 Nov 2017 10:48 |
| Deposited On: | 22 Nov 2017 10:48 |
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