Our news journalists obtained a quote from the research from CEA Saclay, "This fine tuning leads to crystallization because the radius of curvature of the initially bidimensional peptide wall can be increased up to a point where the wall is essentially flat and a crystal is allowed to grow along a third dimension. By comparing X-ray diffraction data and Fourier transform Raman spectra, we show that the nanotubes and the crystals share similar cell parameters and molecular conformations, proving that there is indeed a structural continuum between these two morphologies."
According to the news editors, the research concluded: "These results illustrate a novel approach to crystallization and represent the first step towards the acquisition of an angstrom-resolution structure of the lanreotide nanotubes -sheet assembly."
For more information on this research see: Directing peptide crystallization through curvature control of nanotubes.
The news correspondents report that additional information may be obtained from F. Gobeaux, CEA Saclay, SCBM, iBiTec S, F-91191
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