Langmuir-Blodgett Nanotemplate and Radiation Resistance in Protein Crystals: State of the Art

Crit Rev Eukaryot Gene Expr. 2012;22(3):219-32. doi: 10.1615/critreveukargeneexpr.v22.i3.50.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Monophosphate / analogs & derivatives
  • Adenosine Monophosphate / chemistry
  • Adenosine Monophosphate / radiation effects
  • Crystallization / methods*
  • Dose-Response Relationship, Radiation
  • Models, Molecular
  • Nanostructures / chemistry*
  • Nanotechnology / methods*
  • Proteins / chemistry
  • Proteins / radiation effects
  • Radiation*
  • Synchrotrons / instrumentation
  • Tetrahydrofolate Dehydrogenase / chemistry
  • Tetrahydrofolate Dehydrogenase / radiation effects

Substances

  • Proteins
  • R388
  • Adenosine Monophosphate
  • 3'-(1-butylphosphoryl)adenosine
  • Tetrahydrofolate Dehydrogenase