Crystallization and preliminary crystallographic study of a recombinant phospholipase D from cowpea (Vigna unguiculataL. Walp)
| Autor: | Mireille Rivière, Robert Verger, Anne-Marie Moustacas-Gardies, Abdelkarim Abousalham, Sabine Chenivesse, Chantal Abergel |
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| Rok vydání: | 2001 |
| Předmět: |
chemistry.chemical_classification
Phospholipase D General Medicine Biology Crystallography X-Ray biology.organism_classification Recombinant Proteins law.invention Vigna chemistry.chemical_compound Crystallography Enzyme chemistry Tungstate Structural Biology law Recombinant DNA Molecule Rosales Crystallization Monoclinic crystal system |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 57:320-322 |
| ISSN: | 0907-4449 |
| DOI: | 10.1107/s0907444900020825 |
| Popis: | The plant phospholipase D (PLD) is considered to be a key enzyme involved in various physiological processes such as signal transduction and membrane metabolism. Crystals of the PLD protein from Vigna unguiculata have been produced from the recombinant 768 amino-acid protein. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 157.7, b = 65.6, c = 90.2 A, beta = 111.5 degrees. There is one molecule in the asymmetric unit. Frozen crystals diffract to at least 1.94 A resolution using synchrotron radiation. A search for heavy-atom derivatives using ytterbium and tungstate is currently under way in order to solve the three-dimensional structure. |
| Databáze: | OpenAIRE |
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