3V8A
Thaumatin by Classical Hanging Drop Vapour Diffusion after 18.1 MGy X-Ray dose at ESRF ID29 beamline (Worst Case)
Summary for 3V8A
| Entry DOI | 10.2210/pdb3v8a/pdb |
| Related | 3ALD 3V7V 3V82 3V84 3V87 3V88 3VCE 3VCG 3VCH 3VCI 3VCJ 3VCK |
| Descriptor | Thaumatin I, GLYCEROL (3 entities in total) |
| Functional Keywords | radiation damage, thin film, langmuir-blodgett, lb, plant protein |
| Biological source | Thaumatococcus daniellii (katemfe) |
| Total number of polymer chains | 1 |
| Total formula weight | 22596.42 |
| Authors | Belmonte, L.,Scudieri, D.,Tripathi, S.,Pechkova, E.,Nicolini, C. (deposition date: 2011-12-22, release date: 2012-11-07, Last modification date: 2024-10-09) |
| Primary citation | Belmonte, L.,Pechkova, E.,Tripathi, S.,Scudieri, D.,Nicolini, C. Langmuir-Blodgett nanotemplate and radiation resistance in protein crystals: state of the art. CRIT.REV.EUKARYOT.GENE EXPR., 22:219-232, 2012 Cited by PubMed Abstract: A state-of-the-art review of the role of the Langmuir-Blodgett nanotemplate on protein crystal structures is here presented. Crystals grown by nanostructured template appear more radiation resistant than the classical ones, even in the presence of a third-generation highly focused beam at the European Synchrotron Radiation Facility. The electron density maps and the changes in parameters such as total diffractive power, B-factor, and pairwise R-factor have been discussed. Protein crystals, grown by the Langmuir-Blodgett nanotemplate-based method, proved to be more radiation resistant compared to crystals grown by the classical hanging drop method in terms of both global and specific damage. PubMed: 23140163DOI: 10.1615/CritRevEukarGeneExpr.v22.i3.50 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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