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Langmuir-Blodgett nanotemplate and radiation resistance in protein crystals: state of the art.

Critical reviews in eukaryotic gene expression (2012-11-13)
Luca Belmonte, Eugenia Pechkova, Shailesh Tripathi, Dora Scudieri, Claudio Nicolini
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.

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Sigma-Aldrich
Dihydrofolate Reductase human, ≥80% (SDS-PAGE), recombinant, expressed in E. coli, ≥1 units/mg protein
Sigma-Aldrich
Dihydrofolate Reductase from bovine liver, ~8 U/mL, ammonium sulfate suspension, off-white