Explore the vast range of titles available.

Neutron diffraction is a noncontact method that can measure the rebar strain inside concrete. In this method, rebar strain and stress are calculated using the diffraction profile of neutrons irradiated during a specific time period. In general, measurement accuracy improves with the length of the measurement time. However, in previous studies, the measurement time was determined empirically, which makes the accuracy and reliability of the measurement results unclear. In this study, the relationship between the measurement time and the measurement standard deviation was examined for reinforced concrete specimens under different conditions. The aim was to clarify the accuracy of the measurement of rebar stress using the neutron diffraction method. It was found that if the optical setup of the neutron diffractometer and the conditions of the specimen are the same, there is a unique relationship between the diffraction intensity and the rebar stress standard deviation. Furthermore, using this unique relationship, this paper proposes a method for determining the measurement time from the allowable accuracy of the rebar stress, which ensures the accuracy of the neutron diffraction method.

Scattering techniques represent non-invasive experimental approaches and powerful tools for the investigation of structure and conformation of biomaterial systems in a wide range of distances, ranging from the nanometric to micrometric scale. More specifically, small-angle X-rays and neutron scattering and light scattering techniques represent well-established experimental techniques for the investigation of the structural properties of biomaterials and, through the use of suitable models, they allow to study and mimic various biological systems under physiologically relevant conditions. They provide the ensemble averaged (and then statistically relevant) information under in situ and operando conditions, and represent useful tools complementary to the various traditional imaging techniques that, on the contrary, reveal more local structural information. Together with the classical structure characterization approaches, we introduce the basic concepts that make it possible to examine inter-particles interactions, and to study the growth processes and conformational changes in nanostructures, which have become increasingly relevant for an accurate understanding and prediction of various mechanisms in the fields of biotechnology and nanotechnology. The upgrade of the various scattering techniques, such as the contrast variation or time resolved experiments, offers unique opportunities to study the nano- and mesoscopic structure and their evolution with time in a way not accessible by other techniques. For this reason, highly performant instruments are installed at most of the facility research centers worldwide. These new insights allow to largely ameliorate the control of (chemico-physical and biologic) processes of complex (bio-)materials at the molecular length scales, and open a full potential for the development and engineering of a variety of nano-scale biomaterials for advanced applications.

We describe in this paper the experimental procedure, the data treatment and the quantification of the black body correction: an experimental approach to compensate for scattering and systematic biases in quantitative neutron imaging based on experimental data. The correction algorithm is based on two steps; estimation of the scattering component and correction using an enhanced normalization formula. The method incorporates correction terms into the image normalization procedure, which usually only includes open beam and dark current images (open beam correction). Our aim is to show its efficiency and reproducibility: we detail the data treatment procedures and quantitatively investigate the effect of the correction. Its implementation is included within the open source CT reconstruction software MuhRec. The performance of the proposed algorithm is demonstrated using simulated and experimental CT datasets acquired at the ICON and NEUTRA beamlines at the Paul Scherrer Institut.

Small-angle X-ray and neutron scattering are used to extract structural parameters and derive structural models of macromolecules in solution. The preparation of pure, monodisperse samples and exactly matching solvent blanks is crucial to the experiments' success. Small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS) are techniques used to extract structural parameters and determine the overall structures and shapes of biological macromolecules, complexes and assemblies in solution. The scattering intensities measured from a sample contain contributions from all atoms within the illuminated sample volume, including the solvent and buffer components, as well as the macromolecules of interest. To obtain structural information, it is essential to prepare an exactly matched solvent blank so that background scattering contributions can be accurately subtracted from the sample scattering to obtain the net scattering from the macromolecules in the sample. In addition, sample heterogeneity caused by contaminants, aggregates, mismatched solvents, radiation damage or other factors can severely influence and complicate data analysis, so it is essential that the samples be pure and monodisperse for the duration of the experiment. This protocol outlines the basic physics of SAXS and SANS, and it reveals how the underlying conceptual principles of the techniques ultimately 'translate' into practical laboratory guidance for the production of samples of sufficiently high quality for scattering experiments. The procedure describes how to prepare and characterize protein and nucleic acid samples for both SAXS and SANS using gel electrophoresis, size-exclusion chromatography (SEC) and light scattering. Also included are procedures that are specific to X-rays (in-line SEC–SAXS) and neutrons, specifically preparing samples for contrast matching or variation experiments and deuterium labeling of proteins.

New methods to automatically build models of macromolecular complexes from high-resolution structures or homology models of their subunits or domains against x-ray or neutron small-angle scattering data are presented. Depending on the complexity of the object, different approaches are employed for the global search of the optimum configuration of subunits fitting the experimental data. An exhaustive grid search is used for hetero- and homodimeric particles and for symmetric oligomers formed by identical subunits. For the assemblies or multidomain proteins containing more then one subunit/domain per asymmetric unit, heuristic algorithms based on simulated annealing are used. Fast computational algorithms based on spherical harmonics representation of scattering amplitudes are employed. The methods allow one to construct interconnected models without steric clashes, to account for the particle symmetry and to incorporate information from other methods, on distances between specific residues or nucleotides. For multidomain proteins, addition of missing linkers between the domains is possible. Simultaneous fitting of multiple scattering patterns from subcomplexes or deletion mutants is incorporated. The efficiency of the methods is illustrated by their application to complexes of different types in several simulated and practical examples. Limitations and possible ambiguity of rigid body modeling are discussed and simplified docking criteria are provided to rank multiple models. The methods described are implemented in publicly available computer programs running on major hardware platforms.

Water mobility in cancer cells could be a powerful parameter to predict the progression or remission of tumors. In the present descriptive work, new insight into this concept was achieved by combining neutron scattering and thermal analyses. The results provide the first step to untangle the role played by water dynamics in breast cancer cells (MCF-7) after treatment with a chemotherapy drug. By thermal analyses, the cells were probed as micrometric reservoirs of bulk-like and confined water populations. Under this perspective we showed that the drug clearly alters the properties of the confined water. We have independently validated this idea by accessing the cellular water dynamics using inelastic neutron scattering. Finally, analysis of the quasi-elastic neutron scattering data allows us to hypothesize that, in this particular cell line, diffusion increases in the intracellular water in response to the action of the drug on the nanosecond timescale.

The 1.1 Å, ultrahigh resolution neutron structure of hydrogen/deuterium (H/D) exchanged crambin is reported. Two hundred ninety-nine out of 315, or 94.9%, of the hydrogen atom positions in the protein have been experimentally derived and resolved through nuclear density maps. A number of unconventional interactions are clearly defined, including a potential O─H…π interaction between a water molecule and the aromatic ring of residue Y44, as well as a number of potential C─H…O hydrogen bonds. Hydrogen bonding networks that are ambiguous in the 0.85 Å ultrahigh resolution X-ray structure can be resolved by accurate orientation of water molecules. Furthermore, the high resolution of the reported structure has allowed for the anisotropic description of 36 deuterium atoms in the protein. The visibility of hydrogen and deuterium atoms in the nuclear density maps is discussed in relation to the resolution of the neutron data.

Bacterial nanocellulose (BC)-based composites containing poly(2-hydroxyethyl methacrylate) (PHEMA), poly(methacroylcholine chloride) (PMACC) or poly(methacroylcholine hydroxide) (PMACH) were characterized by inelastic neutron scattering (INS) spectroscopy, combined with DFT (density functional theory) calculations of model systems. A reasonable match between calculated and experimental spectral lines and their intensities was used to support the vibrational assignment of the observed bands and to validate the possible structures. The differences between the spectra of the nanocomposites and the pure precursors indicate that interactions between the components are stronger for the ionic poly(methacrylate) derivatives than for the neutral counterpart. Displaced anions interact differently with cellulose chains, due to the different ability to compete with the O–H···O hydrogen bonds in cellulose. Hence, the INS is an adequate technique to delve deeper into the structure and dynamics of nanocellulose-based composites, confirming that they are true nanocomposite materials instead of simple mixtures of totally independent domains.

Two analytical methods based on the neutrons high penetrability, i.e. neutron diffraction (ND) and neutron computed tomography (NCT) were used to investigate the structure of the aragonitic skeleton of an exemplar/sample of Dipastraea pallida (Dana 1846), a modern hermatypic coral. ND was used to reconstruct the orientation distribution function (ODF) of the crystalline fibrils which compose the coral skeleton. Accordingly, 684 ND spectra were analyzed using the Rietveld method. The result confirmed the aragonite as the sole mineral component of coral skeleton, allowing to recalculate the ODF of aragonite fibrils and to represent it by means of (100), (010) and (001) crystallographic planes pole figures (PF). Experimental PF showed a remarkable similarity with PF recalculated by considering that all aragonite fibrils are oriented either along the growth axis of polyp cups or perpendicular to this direction. This result confirmed the previous observations based on optical microscopy, proving at the same time the availability of ND for such types of investigations. In turn, NCT evidenced the individual polyp cups, their interlocked 3D rigid porous structure as well as a periodic variation of density which could be attributed to a seasonal influence of the marine environment. Different from the classical X-ray computed tomography, the NCT, in view of neutron high cross-section for hydrogen, demonstrated the presence of a small amount of organic matter, otherwise transparent for X- and gamma rays.

Combined neutron scattering and diffusion nuclear magnetic resonance experiments have been used to reveal significant interregional asymmetries (lateralization) in bovine brain hemispheres in terms of myelin arrangement and water dynamics at micron to atomic scales. Thicker myelin sheaths were found in the left hemisphere using neutron diffraction. 4.7 T d MRI and quasi-elastic neutron experiments highlighted significant differences in the properties of water dynamics in the two hemispheres. The results were interpreted in terms of hemisphere-dependent cellular composition (number of neurons, cell distribution, etc.) as well as specificity of neurological functions (such as preferential networking).