Open AccessProtein nanocrystallography: growth mechanism and atomic structure of crystals induced by nanotemplates
Author(s) -
Pechkova E.,
Vasile F.,
Spera R.,
Fiordoro S.,
Nicolini C.
Publication year - 2005
Publication title -
journal of synchrotron radiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.172
H-Index - 99
ISSN - 1600-5775
DOI - 10.1107/s0909049505011647
Subject(s) - protein crystallization , lysozyme , crystallography , chemistry , synchrotron radiation , nucleation , crystal (programming language) , crystal structure , circular dichroism , crystal growth , mass spectrometry , crystallization , chemical physics , organic chemistry , chromatography , optics , computer science , programming language , biochemistry , physics
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 α‐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.