Crystallization and Preliminary X-ray Studies on the Core Proteins of Cellobiohydrolase I and Endoglucanase I from Trichoderma reesei
| Autor: | TT Teeri, Mark J. Bailey, Emilio Margolles-Clark, Jerry Ståhlberg, Christina Divne, T.A. Jones, Göran Pettersson, Irmgard Sinning, M Siikaaho |
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| Rok vydání: | 1993 |
| Předmět: |
Glycoside Hydrolases
Protein Conformation Cellulase Crystallography X-Ray Polyethylene Glycols law.invention Calcium Chloride Structural Biology law Cellulose 1 4-beta-Cellobiosidase Cellobiohydrolase I Crystallization Molecular Biology Trichoderma reesei Trichoderma Endoglucanase I biology Chemistry X-ray Core protein biology.organism_classification Crystallography Ammonium Sulfate biology.protein Indicators and Reagents |
| Zdroj: | Divne, C, Sinning, I, Ståhlberg, J, Pettersson, G, Bailey, M, Siika-aho, M, Margolles-Clark, E, Teeri, T & Jones, A 1993, ' Crystallization and preliminary X-ray studies on the core proteins of cellobiohydrolase I and endoglucanase I from Trichoderma reesei ', Journal of Molecular Biology, vol. 234, no. 3, pp. 905-907 . https://doi.org/10.1006/jmbi.1993.1640 |
| ISSN: | 0022-2836 |
| DOI: | 10.1006/jmbi.1993.1640 |
| Popis: | The catalytic core domains of cellobiohydrolase I (CBHI) and endoglucanase I (EGI) from Trichoderma reesei have been crystallized using the hanging drop vapour diffusion method. In the case of CBHI, use of polyethylene glycol 20,000, and calcium chloride at low pH produced good quality single crystals suitable for X-ray studies. The crystals belong to a primitive orthorhombic space group with unit cell dimensions a = 84·0 Å, b = 86·2 Å, c = 111·8 Å, and diffract beyond 2·0 Å resolution. Bipyramidal crystals of EGI core were grown from ammonium sulphate at pH 7·5. The crystals are tetragonal, either P 4122 or the enantiomorph P4322, with cell dimensions a = b = 101·8 Å and c = 198·0 Å, and at best diffract to a resolution of 2·5 Å. |
| Databáze: | OpenAIRE |
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