Direct observation of local distortion of a crystal lattice with picometer accuracy using atomic resolution neutron holography.

We demonstrate that neutron holography permits us to extend the determination of atomic positions beyond nearest neighbors at least up to the fourth neighboring shell around cadmium probe atoms alloyed into a lead crystal. The accuracy achieved is sufficient to allow quantitative determination of displacements of atoms due to elastic distortions induced by impurity atoms. The atomic positions derived from the holographic data are in good agreement with those expected theoretically due to Friedel oscillations in this system. In addition, the atomic positions are in qualitative agreement with results obtained in an independent experiment studying the diffuse distortion scattering around Bragg peaks.

Investigation of biological macromolecular systems with a pulsed neutron source--a review.

The conclusion that can be drawn on the basis of the above considerations is that investigation of biological macromolecules and crystalline structures by SAS and diffraction of neutrons with the TOF method is feasible. The main difficulties of the TOF method (the wavelength dependence of the incident beam, resolution power, and detector efficiency; the need for their determination and up-to-date values) are compensated for by its advantages. Both methods allow a high data accumulation rate and optimal employment of the incident neutron spectrum. The latter has been achieved by utilizing a dominant part of the Maxwellian spectrum and by a more uniform distribution of statistical accuracy over the most informative measuring range. Another advantage is the high degree of monochronatization of the incident neutron beam by the TOF method. The rigid requirements concerning the data accumulation rate and the capacity of the on-line system computer memory are technical problems but not basic ones.

Temperature and pH dependence of immunoglobulin G conformation.

Previous indirect observations have indicated that IgG may change its conformation at low or high pH and at a temperature of about 35 degrees C. By means of small angle neutron scattering a change in the value of the gyration radius of two different native IgG's was observed above 44 degrees C. No similar change was detected when the sample was previously dissolved in an acidic buffer. The acidic pretreatment caused a significant decrease in the gyration radius (Rg) value measured at 20 degrees C which was partially recovered by increasing the temperature. These observations led to the assumption that the main conformational change observed appears either in the hinge region of the molecular or in the interdomain areas separating the constant and the variable domains of the Fab parts.

Different segmental flexibility of human serum transferrin and lactoferrin.

X-ray diffraction studies show that the diferric (holo) forms of human serum transferrin and lactoferrin have almost the same conformation in crystal. In solution, however, the two proteins exhibit different characteristics. The differences are even more pronounced in the apo forms. Small-angle X-ray and neutron scattering data show that lactoferrin is less compact, in apo and holo forms, than the corresponding forms of transferrin in solution. The comparison of primary structures of the two proteins suggests that one of the interdomain hinge regions is significantly longer in lactoferrin than its counterpart in transferrin. The difference in flexibility due to the long hinge region in lactoferrin may be responsible for many of the differences in the physicochemical characteristics of the two proteins.

Holographic imaging of atoms using thermal neutrons.

In a recent paper [L. Cser, G. Krexner, and Gy. Török, Europhys. Lett. 54, 747 (2001)]] the use of thermal neutrons with wavelengths close to interatomic distances in condensed matter was proposed to obtain holographic images on an atomic scale. Two experimental methods were considered which either put the radiation source inside and the detector outside the object or vice versa. The second approach, called the inside-detector concept, requires strongly neutron-absorbing isotopes acting as pointlike detectors in the sample. In the present work, we demonstrate the feasibility of this technique by recording a holographic image of a lead nuclei in a Pb(Cd) single crystal.

General shape and hapten-induced conformational changes of pig antibody against dinitrophenyl. A small-angle scattering study.

Pig antibodies against dinitrophenyl were studied by neutron small-angle scattering and X-ray small-angle scattering with particular attention to the analysis of cross-section plots and determination of the radii of gyration of cross-section. The experimentally determined molecular parameters Rg (radius of gyration), Rq1 and Rq2 (two different radii of gyration of cross-section characterizing every antibody sample) show that the shapes of the two antibody types, precipitating and non-precipitating, are similar. The non-precipitating antibody is slightly more compact. The parameters Rg, Rq1 and Rq2 of complexes of antibodies with the hapten, 8-dinitrophenyl-5,8-aza-4-oxo-octanoic acid, are smaller than those of the free antibody. This indicates that a conformational change is induced by the binding of the hapten. The character of the change of parameters is consistent with a view that the observed contraction of the molecule proceeds via similarity transformation. In order to design a model of a pig antibody molecule, isolated building blocks of the molecule, the Fab and Fc fragments, were first studied. A comparison of the scattering curves with various models of fragments showed, however, that the isolated fragments acquire in solution elongated rod-like shapes. Over 300 tentative models of the intact antibody molecule, built of small identical spheres, were constructed before a good fit with the experimental data was achieved. The most probable models have a cavity in the Fc part and the Fab parts are either fully extended or slightly bent downwards to the Fc part.