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http://ipicyt.repositorioinstitucional.mx/jspui/handle/1010/1199| Expression, purification and preliminary crystallization of amaranth 11S proglobulin seed storage protein from Amaranthus hypochondriacus L. | |
| LAURA DENNISSE CARRAZCO PEÑA ANA PAULINA BARBA DE LA ROSA | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| https://doi.org/10.1107/S1744309110021032 | |
| Seed storage proteins Amaranthus hypochondriacus L. Amaranth 11S proglobulin | |
| "11S globulin is one of the major seed storage proteins in amaranth. Recombinant protein was produced as up to similar to 80% of the total bacterial protein using Escherichia coli Rosetta-gami (DE3) containing pET21d with amaranth 11S globulin cDNA. The best expression condition was at 302 K for 20 h using LB medium containing 0.5 M NaCl. The recombinant protein was easily separated from most of the Escherichia coli proteins by precipitation with 0-40% ammonium sulfate solution. It formed aggregates at low temperature and at low salt concentrations. This behaviour may imply that it has a more hydrophobic nature than other 11S seed globulins. The crystals diffracted to 6 A resolution and belonged to space group P6(3), with unit-cell parameters a = b = 97.6, c = 74.8 A, gamma = 120.0 degrees. One subunit of a trimer was estimated to be present in the asymmetric unit, assuming a V (sol) of 41%. To obtain the complete structure solution, experiments to improve crystallization and flash-cooling conditions are in progress." | |
| International Union of Crystallography | |
| 2010-08 | |
| Artículo | |
| Inglés | |
| Tandang-Silvas, M. R., Carrazco-Pena, L., Barba de la Rosa, A. P., Osuna-Castro, J. A., Utsumi, S., Mikami, B. & Maruyama, N. (2010). Acta Cryst. F66, 919-922. | |
| BIOLOGÍA Y QUÍMICA | |
| Versión publicada | |
| publishedVersion - Versión publicada | |
| Aparece en las colecciones: | Publicaciones Científicas Biología Molecular |
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