title: Protein nanocrystallography: growth mechanism and atomic structure of crystals induced by nanotemplates.
abstract: Protein nanocrystallography, a new technology for crystal growth based on protein nanotemplates, has recently been shown to produce diffracting, stable and radiation-resistant lysozyme crystals. This article, by computing these lysozyme crystals' atomic structures, obtained by the diffraction patterns of microfocused synchrotron radiation, provides a possible mechanism for this increased stability, namely a significant decrease in water content accompanied by a minor but significant alpha-helix increase. These data are shown to be compatible with the circular dichroism and two-dimensional Fourier transform spectra of high-resolution H NMR of proteins dissolved from the same nanotemplate-based crystal versus those from a classical crystal. Finally, evidence for protein direct transfer from the nanotemplate to the drop and the participation of the template proteins in crystal nucleation and growth is provided by high-resolution NMR spectrometry and mass spectrometry. Furthermore, the lysozyme nanotemplate appears stable up to 523 K, as confirmed by a thermal denaturation study using spectropolarimetry. The overall data suggest that heat-proof lysozyme presence in the crystal provides a possible explanation of the crystal's resistance to synchrotron radiation.
authors.affiliation: Fondazione ElBA, Via delle Testuggini, Roma, Italy.
authors.forename: E
authors.initials: E
authors.lastname: Pechkova
authors.forename: F
authors.initials: F
authors.lastname: Vasile
authors.forename: R
authors.initials: R
authors.lastname: Spera
authors.forename: S
authors.initials: S
authors.lastname: Fiordoro
authors.forename: C
authors.initials: C
authors.lastname: Nicolini
mesh_terms: D000818:Animals; D002645:Chickens; D003460:Crystallization / Q000379:methods*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D013058:Mass Spectrometry; D009113:Muramidase / Q000737:chemistry*; D036103:Nanotechnology / Q000379:methods*
chemical_list: D009113:Muramidase