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3VCE

Thaumatin by LB based Hanging Drop Vapour Diffusion after 18.1 MGy X-Ray dose at ESRF ID29 beamline (Best Case)

Summary for 3VCE
Entry DOI10.2210/pdb3vce/pdb
Related3ALD 3V7V 3V82 3V84 3V87 3V88 3V8A 3VCG 3VCH 3VCI 3VCJ 3VCK
DescriptorThaumatin I, GLYCEROL (3 entities in total)
Functional Keywordsradiation damage, thin film, langmuir-blodgett, lb, plant protein
Biological sourceThaumatococcus daniellii (katemfe)
Total number of polymer chains1
Total formula weight22596.42
Authors
Belmonte, L.,Pechkova, E.,Scudieri, D.,Nicolini, C. (deposition date: 2012-01-04, release date: 2012-11-21, Last modification date: 2024-10-30)
Primary citationBelmonte, 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: 23140163
DOI: 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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