Purification, crystallization and initial X-ray analysis of the C1subunit of the astaxanthin protein, V600,of the chondrophoreVelella velella
| Autor: | P.F. Zagalsky, T. J. Boggon, James Raftery, John R. Helliwell, Naomi E. Chayen |
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| Rok vydání: | 1999 |
| Předmět: |
Ammonium sulfate
biology Hydra Protein Conformation Protein subunit X-ray General Medicine Xanthophylls Crystallography X-Ray beta Carotene biology.organism_classification law.invention chemistry.chemical_compound Crystallography Protein structure chemistry Structural Biology Astaxanthin law Animals Velella Crystallization X ray analysis |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 55:266-268 |
| ISSN: | 0907-4449 |
| DOI: | 10.1107/s0907444998006908 |
| Popis: | The subunit C1 of the carotenoid-binding protein, V600, of the chondrophore Velella velella has been purified and crystallized. The crystals, which were grown by the vapour-diffusion method from ammonium sulfate as the major precipitant, diffract beyond 3 A and show little radiation damage over long periods (greater than 100 h) on a Cu Kalpha rotating-anode X-ray source. The space group of the crystals is P212121 with cell dimensions a = 42.0, b = 80.9, c = 110. 6 A. |
| Databáze: | OpenAIRE |
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