Crystallization and Preliminary X-ray Data of Chloromuconate Cycloisomerase from Alcaligenes eutrophus JMP134 (pJP4)
| Autor: | Helga Hoier, Thomas Hildenbrand, Angela Hammer, Michael Schlömann, John J. Stezowski, Ka-Leung Ngai |
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| Rok vydání: | 1993 |
| Předmět: |
Crystallography
Chemistry Chloromuconate cycloisomerase Resolution (electron density) Alcaligenes eutrophus law.invention Tetragonal crystal system Bipyramid Bacterial Proteins X-Ray Diffraction Structural Biology law X-ray crystallography X ray data Alcaligenes Crystallization Intramolecular Lyases Isomerases Molecular Biology |
| Zdroj: | Journal of Molecular Biology. 232:305-307 |
| ISSN: | 0022-2836 |
| DOI: | 10.1006/jmbi.1993.1385 |
| Popis: | The pJP4-encoded chloromuconate cycloisomerase, an enzyme of the 2,4-dichlorophenoxy-acetate degradation pathway, was purified from cell free extracts of Alcaligenes eutrophus JMP134 with a revised procedure. Tetragonal bipyramidal crystals were grown and characterized with respect to their X-ray diffraction properties. They were assigned to the space group I 4, with cell dimensions of a = b = 111·9 A, c = 148·5 A. The crystals scattered to approximately 3 A resolution. |
| Databáze: | OpenAIRE |
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