Título
Expression, purification and preliminary crystallization of amaranth 11S proglobulin seed storage protein from Amaranthus hypochondriacus L.
Autor
LAURA DENNISSE CARRAZCO PEÑA
ANA PAULINA BARBA DE LA ROSA
Nivel de Acceso
Acceso Abierto
Identificador alterno
doi: https://doi.org/10.1107/S1744309110021032
Materias
Resumen o descripción
"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."
Editor
International Union of Crystallography
Fecha de publicación
agosto de 2010
Tipo de publicación
Artículo
Versión de la publicación
Versión publicada
Recurso de información
Formato
application/pdf
Idioma
Inglés
Relación
&
Maruyama, N. (2010). Acta Cryst. F66, 919-922.
Sugerencia de citación
Tandang-Silvas, M. R., Carrazco-Pena, L., Barba de la Rosa, A. P., Osuna-Castro, J. A., Utsumi, S., Mikami, B.
Repositorio Orígen
Repositorio IPICYT
Descargas
398