Crystallization and Preliminary X-ray Investigation of a Recombinant Outer Membrane Protein from Neisseria meningitidis
| Autor: | Ines M. Li De La Sierra, Thierry Prangé, Alexis Musacchio, Roger Fourme, Pablo Fuentes, Juan Madrazo, Gabriel Padrón |
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| Rok vydání: | 1994 |
| Předmět: |
Antigens
Bacterial Resolution (electron density) X-ray Synchrotron radiation Neisseria meningitidis Crystallography X-Ray Recombinant Proteins law.invention chemistry.chemical_compound Tetragonal crystal system Crystallography Monomer chemistry Structural Biology law X-ray crystallography Crystallization Bacterial outer membrane Molecular Biology Bacterial Outer Membrane Proteins |
| Zdroj: | Journal of Molecular Biology. 235:1154-1155 |
| ISSN: | 0022-2836 |
| DOI: | 10.1006/jmbi.1994.1067 |
| Popis: | A protein constituent of the outer membrane from Neisseria meningitidis (hereafter called P64K) has been crystallized using the hanging drop technique. Crystals are tetragonal with unit cell dimensions a = b = 136·84 A and c = 78·44 A, compatible with a single monomer of 64 kDa in the asymmetric unit. When exposed to high intensity synchrotron radiation, these crystals diffract X-rays to at least 2·9 A resolution, indicating that a high resolution structure analysis is feasible. |
| Databáze: | OpenAIRE |
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