dc.contributorInternational Union of Crystallography
dc.creatorCarrazco Peña, Laura Dennisse
dc.creatorBarba de la Rosa, Ana Paulina
dc.date2018-03-23T23:59:26Z
dc.date2018-03-23T23:59:26Z
dc.date2010-08
dc.date.accessioned2023-07-17T22:04:12Z
dc.date.available2023-07-17T22:04:12Z
dc.identifierTandang-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.
dc.identifierhttp://hdl.handle.net/11627/3689
dc.identifierhttps://doi.org/10.1107/S1744309110021032
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7543862
dc.description"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."
dc.formatapplication/pdf
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rightsAcceso Abierto
dc.subjectSeed storage proteins
dc.subjectAmaranthus hypochondriacus L.
dc.subjectAmaranth 11S proglobulin
dc.subjectBIOLOGÍA Y QUÍMICA
dc.titleExpression, purification and preliminary crystallization of amaranth 11S proglobulin seed storage protein from Amaranthus hypochondriacus L.
dc.typearticle


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