The high accuracy of X-ray analyses at atomic resolution is now able to display subtle deformations from standard geometry of building blocks in proteins. From the analysis of nine ultra-high resolution protein structures, we derived the first experimental evidence that a significant pyramidalization at the main-chain carbonyl carbon atom occurs in proteins. Our findings also show that this pyramidalization is related to the main-chain ψ torsion angle. The carbonyl carbon atoms of residues that adopt αR and extended conformations show a clear preference for positive and negative pyramidalization, respectively. The agreement between our data and those previously obtained from small molecule structures demonstrates that carbon pyramidalization is an intrinsic property of the peptide structure. Although small in magnitude, the pyramidalization is well preserved in the complex folded state of a macromolecular structure that results from the interplay of many different forces. In addition, this property of the peptide group may have interesting implications for the enzymatic reactions involving the carbonyl carbon atoms.

One of the atomic-focuser modes for ultra-high resolution electron microscopy is described theoretically and illustrated by the observation of images formed within the diffraction spots of nanodiffraction patterns of carbon nanoshells. In this mode, the specimen is illuminated by the focused probe of a scanning transmission electron microscope and is followed by a thin crystal at a Fourier-image distance. The theory shows that each diffraction spot of the crystal contains a magnified image of the illuminated area of the specimen, having a resolution depending on the width of the intensity peak of electrons channeled along atomic rows in the crystal. A thin graphite crystal, contained within one wall of a carbon nanoshell, can act as an atomic focuser to image part of the other wall of the nanoshell, or tungsten atoms deposited on this wall. Simulations of the transmission of electrons through graphite crystals show that the images formed should have a resolution of about 0.06 nm. Experimental images suggest that this resolution has been attained in the imaging of tungsten atoms or clusters of tungsten atoms.