The structure and continuous stoichiometry change of 1DTbBrx@SWCNTs.

HRTEM and HAADF STEM of 1DTbBrx@SWCNT meta-nanotubes reveal three structural modifications of 1D nanocrystals within single wall carbon nanotube channels attributed to a different stoichiometry of the guest crystal. For SWCNTs with diameters Dm > 1.4 nm a most complete tetragonal unit cell is observed. When crystallization occurs inside SWCNT with Dm < 1.4 nm 1D TbBrx crystal deforms a nanotube to elliptical shape in cross section. In this case the 1D crystal unit cell becomes monoclinic, with possible loss of a part of bromine atoms. Two modifications of a monoclinic unit cell appear. One of them is characterized by single or pair vacancies in the structure of the 1D crystal. Another structure is explained by peripheral and central bromine atoms loss. An appearance of such modifications can be stimulated by electron irradiation. The loss of bromine atoms is in agreement with chemical analysis data. Electronic properties of obtained meta-nanotubes are investigated using optical absorption and Raman spectroscopy. It is shown that intercalation of terbium bromide into SWCNTs leads to acceptor doping of SWCNTs. According to local EDX analysis and elemental mapping this doping can arise from significant stoichiometry change in 1D nanocrystal indicating an average Tb:Br atomic ratio of 1:2.8 ± 0.1.

Genome packaging in EL and Lin68, two giant phiKZ-like bacteriophages of P. aeruginosa.

A unique feature of the Pseudomonas aeruginosa giant phage phiKZ is its way of genome packaging onto a spool-like protein structure, the inner body. Until recently, no similar structures have been detected in other phages. We have studied DNA packaging in P. aeruginosa phages EL and Lin68 using cryo-electron microscopy and revealed the presence of inner bodies. The shape and positioning of the inner body and the density of the DNA packaging in EL are different from those found in phiKZ and Lin68. This internal organization explains how the shorter EL genome is packed into a large EL capsid, which has the same external dimensions as the capsids of phiKZ and Lin68. The similarity in the structural organization in EL and other phiKZ-like phages indicates that EL is phylogenetically related to other phiKZ-like phages, and, despite the lack of detectable DNA homology, EL, phiKZ, and Lin68 descend from a common ancestor.

HRTEM of 1DSnTe@SWNT nanocomposite located on thin layers of graphite.

The method for imaging of highly sensitive nanostructures unstable under electron beam irradiation is introduced. To reduce charge and thermally generated beam damage, highly conductive multilayered graphene or thin graphite layers were used as supports for nanostructures. Well-defined crystalline structure of graphite layers enables image reconstruction by Fourier filtering and allows maintaining high quality of images. The approach was tested for imaging of highly sensitive quasi one-dimensional SnTe nanocrystals hosted inside single-walled carbon nanotubes. Relying on the filtered images and the image simulation, the structure of one-dimensional SnTe was established as a chain of fcc NaCl type unit cells, connected by the [001] edges with <110> direction coinciding with nanotube axis.

The structure of nanocomposite 1D cationic conductor crystal@SWNT.

Nanocomposites consisting of one-dimensional (1D) crystals of the cationic conductors CuI, CuBr and AgBr inside single-walled carbon nanotubes, mainly (n, 0), were obtained using the capillary technique. 1D crystal structure models were proposed based on the high resolution transmission electron microscopy performed on a FEI Titan 80-300 at 80 kV with aberration correction. According to the models and image simulations there are two modifications of 1D crystal: hexagonal close-packed bromine (iodine) anion sublattice (growth direction <001>) and 1D crystal cubic structure (growth direction <112>) compressed transversely to the nanotube (D(m) ∼1.33 nm) axis. Tentatively this kind of 1D crystal can be considered as monoclinic. One modification of the anion sublattice reversibly transforms into the other inside the nanotube, probably initiated by electron beam heating. As demonstrated by micrographs, copper or silver cations can occupy octahedral positions or are statistically distributed across two tetrahedral positions. A 1DAgBr@SWNT (18, 0; 19, 0) pseudoperiodic 'lattice distortion' is revealed resulting from convolution of the nanotube wall function image with 1D cubic crystal function image.

The structure of 1D CuI crystals inside SWNTs.

Nanocomposites consisting of one-dimensional CuI crystals inside single-walled carbon nanotubes were obtained using the capillary technique. high-resolution transmission electron microscopy investigations of the atomic structure of the encapsulated 1D CuI crystals revealed two types of 1D CuI crystals with growth direction <001> and <110> relative to the bulk hexagonal CuI structure. Atomic structure models were proposed based on the high-resolution transmission electron microscopy images. According to the proposed models and image simulations, the main contrast in the 1D crystal images arises from the iodine atoms whereas copper atoms, with lower atomic number giving lower contrast, are thought to be statistically distributed.

TEM and HREM of diamond crystals grown on Si tips: structure and results of ion-beam-treatment.

Diamond single crystals were grown on the silicon whiskers by a hot filament chemical vapor deposition technique at the filament temperature about 2100 degrees C and the temperature of support 800 degrees C. Specimens were examined by SEM, TEM, HRTEM and SAED. When the filament temperature was about 1900 degrees C globular polycrystalline diamond particles were grown. At a support temperature more then 800 degrees C SiC nanoparticles were formed. To investigate the ion etching process of the silicon tip/diamond system, tips were treated with an Ar(+) beam with energy up to 30 kV. The results depend on fluence: at 4 x 10(18)ion/cm(2) diamonds and partially Si tips were destroyed, amorphous layer was formed (sometimes with nanometric size fragments of diamond); at 1 x 10(18)ion/cm(2) sharpened diamonds (radius of curvature about 20 nm) covered with amorphous layer (radius about 80 nm) probably with nanoclusters of diamond were observed; at 4.4 x 10(17) ion/cm(2) there was no visible tip sharpening but formation of amorphous thick layer occurred. The emission characteristics of Si tips covered with diamond were improved due to ion treatment. Since such tips in our case were covered with amorphous layer containing nanometric size fragments of diamond, we suppose this layer is responsible for electron emission improvement.

Three-dimensional structure of infectious bursal disease virus determined by electron cryomicroscopy.

Infectious bursal disease virus (IBDV), a member of the Birnaviridae group, is a commercially important pathogen of chickens. From electron micrographs of frozen, hydrated, unstained specimens, we have computed a three-dimensional map of IBDV at about 2 nm resolution. The map shows that the structure of the virus is based on a T=13 lattice and that the subunits are predominantly trimer clustered. The subunits close to the fivefold symmetry axes are at a larger radius than those close to the two- or threefold axes, giving the capsid a markedly nonspherical shape. The trimer units on the outer surface protrude from a continuous shell of density. On the inner surface, the trimers appear as Y-shaped units, but the set of units surrounding the fivefold axes appears to be missing. It is likely that the outer trimers correspond to the protein VP2, carrying the dominant neutralizing epitope, and the inner trimers correspond to protein VP3, which has a basic carboxy-terminal tail expected to interact with the packaged RNA.

Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy.

Human hepatitis B virus core protein expressed in E. coli assembles into two sizes of particle. We have determined their three-dimensional structures by electron cryomicroscopy and image processing. The large and small particles correspond to triangulation number T = 4 and T = 3 dimer clustered packings, containing 240 and 180 protein subunits, respectively. The local packing of subunits is very similar in the two sizes of particle and shows holes or channels through the shell. The native viral core particle packages RNA and is active in reverse transcription to DNA. The holes we observe may provide access for the necessary small molecules. Shells assembled from the intact core protein contain additional material, probably RNA, which appears as an icosahedrally ordered inner shell in the three-dimensional map.

[Results of the use of a graft with a monocusp in radical correction of Fallot's tetrad]. / Rezul'taty primeneniia zaplaty s monostvorkoi pri radikal'noi korrektsii tetrady Fallo.

The article deals with the results of complex study of the effect of pulmonary insufficiency on intracardiac hemodynamics and function of the heart in the immediate and late-term periods after radical correction of Fallot's tetralogy. Answers are also given to questions concerning the expediency of the use and functional adequacy of a xeno-pericardial monocusp in the closure mechanism of the pulmonary artery valve. The study showed that massive pulmonary regurgitation has a negative effect on the functional condition of the right ventricle in late-term postoperative periods. Convincing data were obtained which allow a graft with a monocusp of a bull's pericardium to be recommended for further clinical use to prevent insufficiency of the pulmonary artery valve after radical correction of Fallot's tetralogy.

Negative staining of proteins.

Negative staining, some closely related alternative preparation techniques and radiation stability are considered. An attempt is made to clarify the mechanism of action and ultimate resolution limit of negative staining. The results of electron diffraction investigation of thermitase microcrystals embedded in glucose and glucose + stains are presented. It is shown that at doses not exceeding 10 electrons/nm2 electron diffraction from thermitase crystals demonstrate diffraction fields up to 0.2 nm. When adding heavy-atom salts to glucose or using negative staining, the relative intensities of reflections change and electron diffraction patterns for every type of heavy-atom additive (or negative stain) have their specific features. Such characteristic changes of reflection intensities indicate specific interaction of these additives (or stains) with the object. In the case of electron diffraction from the crystals stained using the routine negative staining technique the ordering was preserved down to 0.4-0.5 nm. Increasing the dose up to the normal value results in fading of distant reflections. Thus, negative staining with radiation doses less than the critical one could yield resolution down to 0.4 nm. Yet, the structure may change due to interaction with the stain. Nevertheless, the possibility that such resolution could be obtained for a limited number of objects should not be excluded. Some examples of the application of negative staining for investigation of quaternary and domain structure of proteins (nitrogenase, glutamine synthetase, mitochondrial ATP-synthase, membrane monooxygenase enzymes), tubular and two-dimensional protein crystals (catalase, phosphorylase, HWV protein, hydrogenase), as well as ribosomes and bacteriophages are given in the review.

Fine structure of the 30 S ribosomal subunit.

Elongated hollow strands were revealed on raw images and averaged by the correlation method images of the 30 S subunit of the E. coli ribosome negatively stained by uranyl acetate. The tentative three-dimensional arrangement of the 'strands' and their nature are discussed.

Electron microscopy of the Mo-Fe-protein from Azotobacter vinelandii nitrogenase.

The quaternary structure of the Mo-Fe-protein from Azotobacter vinelandii has been studied by electron microscopy. A model of the molecule of the Mo-Fe-protein has been proposed: two alpha subunits are displaced relative to two beta subunits along a twofold axis, so the molecule can be characterized by the point-group pseudosymmetry 222. Computer averaging of the images showed that one of the projections of the molecule could be characterized by twofold rotational symmetry. Micrographs of nitrogenase recombined complex (Mo-Fe-protein + Fe-protein) have been obtained. They showed particles close in size and form to the Mo-Fe-protein molecule. Therefore, it has been proposed that the Fe-protein could be situated in the central cavity of Mo-Fe-protein.

On the negative straining of the protein crystal structure.

It has been shown that in some cases negative staining reveals structure with details down to 0.4 nm in size, the nature of protein playing a key role. Various stains seem to interact with different parts of a thermitase (a serine protease) molecule, which results in intensity changes in electron diffraction patterns.

Electron microscope study on human ceruloplasmin.

Electron microscopy of human ceruloplasmin (CP) molecules revealed a few distinctive types of particle images. Analysis of these images allows to propose a tentative model for CP: six "subunits" (which we call domains) not much different in size are arranged with 32 point group pseudosymmetry. The determination of the number of polypeptides arising at the spontaneous specific proteolytic fragmentation of CP and their molecular weights conform with this assumption. The electrophoretic studies of the CP samples prepared both with and without potent proteolytic inhibitor, PMSF, revealed that CP is a single-chain protein with molecular weight of 130 000. Isolated and stored without PMSF the polypeptide chain of CP undergoes specific proteolytic cleavage which results in the appearance of polypeptides with molecular weights of 16 000, 48 000, and 64 000. The latter two polypeptides degradate to about two- and three-fold decreased molecular weights fragments, respectively. Therefore, the single polypeptide chain of CP contains at least five peptide bonds which are particularly susceptible to proteolytic attack and which connect six principal segments of the chain. The hydrolysis of these bonds results in liberation of the six fragments which were integrated in the enzymatically active globule of CP.