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Bacterial cellulose (BC) is synthesized and exported through the cell membrane via a large protein complex (terminal complex) that consists of three or four subunits. BcsC is a little-studied subunit considered to export BC to the extracellular matrix. It is predicted to have two domains: a tetratrico peptide repeat (TPR) domain and a β-barrelled outer membrane domain. Here we report the crystal structure of the N-terminal part of BcsC-TPR domain (Asp24–Arg272) derived from Enterobacter CJF-002. Unlike most TPR-containing proteins which have continuous TPR motifs, this structure has an extra α-helix between two clusters of TPR motifs. Five independent molecules in the crystal had three different conformations that varied at the hinge of the inserted α-helix. Such structural feature indicates that the inserted α-helix confers flexibility to the chain and changes the direction of the TPR super-helix, which was also suggested by structural analysis of BcsC-TPR (Asp24–Leu664) in solution by size exclusion chromatography-small-angle X-ray scattering. The flexibility at the α-helical hinge may play important role for exporting glucan chains.

Time-resolved x-ray diffraction studies have been made on the 5.9- and 5.1-nm actin layer lines from frog skeletal muscles during an isometric tetanus at 6 degrees C, using synchrotron radiation. The integrated intensities of these actin layer lines were found to increase during a tetanus by 30-50% for the 5.9-nm reflection and approximately 70% for the 5.1-nm reflection of the resting values. The intensity increase of both reflections was greater than that taking place in the transition from rest to rigor state. The intensity change of the 5.9-nm reflection preceded those of the myosin 42.9-nm off-meridional reflection and of the equatorial reflections, as well as the isometric tension development. The intensity profile of the 5.9-nm layer line during contraction was found to be different from that observed in the rigor state.

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Compacted Na-bentonite, of which the major mineral is montmorillonite, is a candidate buffer material for the geological disposal of high-level radioactive waste. A potential alteration of the bentonite in a repository is the partial replacement of the exchangeable cations of Na However, the apparent diffusion coefficient of Ca 2+ and the activation energy for diffusion at the same dry density were independent of the ionic equivalent fraction of Ca 2+ ions. These findings suggest that unlike HTO, which can be postulated to diffuse mainly in pore water, Ca 2+ ion diffusion could occur predominantly in interlayer spaces, of which the basal spacing was determined to be constant by the XRD technique.

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For performance assessments of geological disposal of high-level radioactive waste, activation energies for the diffusion of strontium ions and the basal spacings of compacted sodium montmorillonite in the water-saturated state were determined.Basal spacings determined by XRD indicated changes in the interlamellar space from a three-water layer hydrate state to a two-water layer hydrate state as the dry density of the montmorillonite increased from 1.0 to 1.8 Mg m-3. Activation energies from 17.3 to 30.8 kJ mol-1 for the apparent diffusion coefficients of strontium ions were obtained. The lower activation energies than for diffusion of strontium ions in free water were determined for montmorillonite specimens of lower dry density (1.2 Mg m-3 and below), while the higher activation energies were at higher dry densities (1.4 Mg m-3 and above).These findings cannot be explained by changes in only the geometric parameters, which the pore water diffusion model is based upon. Possible explanations for the dry density dependence of the activation energy are the changes of the temperature dependence of the distribution coefficients and/or of the diffusion process with increasing dry density