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The spectrum and angular distribution of x rays scattered from a water phantom.

To calculate the response of an image receptor to the x rays emerging from a scattering medium, it is necessary to know the x-ray spectrum and intensity as a function of the angle of incidence on the receptor. To permit this calculation for any x-ray spectrum incident on a medium, these functions must be known for monoenergetic x rays. For monoenergetic x rays in the range 20-70 keV we have measured with a high-purity germanium detector the spectrum and intensity of x rays emitted from a water phantom at angles of 0 degree-50 degrees to the direction of the primary beam. The spectrum and intensity of emitted x rays have also been calculated by the Monte Carlo method. At small exit angles, most of the x rays have energies close to the incident energy. As the exit angle increases, the fraction of multiply scattered x rays increases. At very large exit angles, the dominant feature of the spectrum is the peak due to these multiply scattered x rays. For small scattering angles the Monte Carlo calculations are in good agreement with the measurements over the range of energies. For large scattering angeles the scattered photon fluence predicted by Monte Carlo modeling is consistently lower than the measurement in the region just below the full energy peak. The cause of the discrepancies is not fully understood, but cannot be accounted for by Compton broadening alone. An alternate approach to model incoherent scattering is proposed.

Humans↗

Relaxation of hot quasiparticles in a d-wave superconductor.

Motivated by recent pump-probe experiments we consider the processes by which "hot" quasiparticles produced near the antinodes of a d-wave superconductor can relax. We show that in a large region of momentum space processes which break Cooper pairs are forbidden by energy and momentum conservation. Equilibration then occurs by scattering with thermal quasiparticles: Umklapp scattering is exponentially suppressed at low temperatures, but small-angle scattering leads to power-law behavior. By solving the Boltzmann equation analytically we make detailed predictions for the temperature and intensity dependence of these processes, which we compare with experiment.

Journal Article↗

Long-range correlations in the speckle patterns of directed waves.

We develop a general method for calculating statistical properties of the speckle pattern of coherent waves propagating in disordered media. In some aspects this method is similar to the Boltzmann-Langevin approach for the calculation of classical fluctuations. We apply the method to the case where the incident wave experiences many small angle scattering events during propagation, but the total angle change remains small. In many aspects our results for this case are different from results previously known in the literature. The correlation function of the wave intensity at two points separated by a distance r, has a long-range character. It decays as a power of r and changes sign. We also consider sensitivities of the speckles to changes of external parameters, such as the wave frequency and the incidence angle.

Journal Article↗

Medical applications of diffraction enhanced imaging.

We have developed a new X-ray imaging technique, diffraction enhanced imaging (DEI), which can be used to independently visualize the refraction and absorption of an object. The images are almost completely scatter-free, allowing enhanced contrast of objects that develop small angle scattering. The combination of these properties has resulted in images of mammography phantoms and tissues that have dramatically improved contrast over standard imaging techniques. This technique potentially is applicable to mammography and other fields of medical X-ray imaging and to radiology in general, as well as possible use in nondestructive testing and X-ray computed tomography. Images of various tissues and materials are presented to demonstrate the wide applicability of this technique to medical and biological imaging.

Journal Article↗

On small angle multiple coulomb scattering of protons in the gaussian approximation.

Experimental data from the literature on small-angle multiple Coulomb scattering of protons in various materials were analysed in order to device an equation for the scattering angle in the Gaussian approximation. In comparison to Highland's well-known formula, the present approximation can be integrated to take into account energy loss in the scattering media. In addition, it is more precise than Highland's formulation for thin and thick scatterers consisting of elements with low atomic number. The simple equation obtained in this study can be used to obtain prompt answers for scattering problems which can occur, for example, in proton therapy or proton radiography.

Models, Theoretical↗

Preliminary X-ray studies on Serratia protease.

Preliminary X-ray studies on Serratia protease have been carried out using crystallographic and small angle scattering techniques. The enzyme has been crystallized in three different crystalline forms by microdialysis and vapor diffusion methods using 50 mM phosphate buffer, pH 6.0, at 24 degrees C. They have orthorhombic space groups: C222(1) for one form and P2(1)2(1)2(1) for the other two forms. A small angle X-ray scattering study showed that the radius of gyration and the maximal dimension of the molecule in aqueous solution are 26.6 A and 94.5 A, respectively. The molecular weight of the enzyme was determined to be 45,000-48,000 by various physical methods.

Crystallography↗

Investigation of the shape and size of myosin subfragment 1 using small-angle X-ray scattering.

Measurement of x-ray scattering at very small angles by solutions of myosin subfragment 1 (S1) yields a radius of gyration of 3.24 nm (mean) +/- 0.03 nm (standard error for N = 9). If S1 is assumed to be ellipsoid of revolution, of uniform electron density, with a molecular weight of 1.15 X 10(5) and a partial specific volume of 0.73 cm3 g-1, then the axial ratio of the ellipsoid is 2.89 +/- 0.06 (prolate) or 0.26 +/- 0.01 (oblate), and the major axis is 13.0 +/- 0.2 nm (prolate) or 10.1 +/- 0.1 nm (oblate). Measurements at larger angles allow models of S1 morphology to be tested; theoretical scattering curves for various ellipsoids of revolution were calculated. The observed scatterina can be approximated by the scattering from ellipsoids with axial ratio 2.0 to 3.0 (prolate), or 0.25 to 0.4 (oblate). Models that fit the data over the range of scattering angles from 0 to 30 mrad are: prolate ellipsoid with axial ratio 2.3, major axis 12 nm; and oblate ellipsoid with axial ratio 0.4 and major axis 10 nm. Thus analyses of two parts of the scattering curve, by different methods, indicate that S1 is fae from spherical, and that its morphology may be approximated by ellipsoids of the aforesaid dimensions.

Models, Chemical↗

Subunit structure of casein micelles from small-angle neutron-scattering.

Wet pellets of whole casein micelles of cows' milk have been studied by small-angle neutron-scattering. Contrast variation using 2H2O/H2O mixtures showed that the previously observed inflection in scattered intensity at Q[4 pi sin theta)/gamma) = 0.035 A-1 is due primarily to scattering from protein, and not from calcium phosphate. Agreement between measured scattering and that calculated for a simple model of packed protein subunits suggests that the whole micelle contains protein subunits of the approximate size of free casein submicelles, packed in a short-range ordered arrangement.

Animals↗

Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask.

Large ATP-dependent proteolytic complexes carry out the majority of intracellular proteolysis. To begin to understand the function of these proteases at a structural level, we have combined the information from a number of biophysical techniques such as electron microscopy (EM), small-angle scattering, and x-ray crystallography. In this study, we exploited the inherent symmetry of Escherichia coli ClpP, the proteolytic component of the ClpAP/XP ATP-dependent protease, to determine its x-ray crystal structure to 2.3-A resolution starting with a phase set derived from a low-resolution mask obtained from EM and small-angle x-ray scattering analysis. Sevenfold and 14-fold noncrystallographic symmetry averaging facilitated phase extension beyond 20 A and in combination with mask redetermination and matrix refinement was sufficient for completely determining the structure. The structure of ClpP is a homo-tetradecamer composed of two heptameric rings enclosing a cavity of approximately 50 A in diameter that compartmentalizes the 14 serine proteolytic active sites. Comparison of the ClpP structure with those of the 20S proteasome and HslV reveals a striking example of evolutionary convergence, despite them being unrelated in sequence and fold. Moreover, similarity in their overall architecture suggests a common model for their action.

Adenosine Triphosphatases↗

Structure of bacteriophage T7. Small-angle X-ray and neutron scattering study.

Small-angle x-ray and neutron scattering techniques were applied to bacteriophage T7 solutions at different scattering densities. Scattering curves determined under a variety of experimental conditions were used to derive a set of parameters characterizing the shape, size, and weight of the whole phage particle and of its DNA and protein components. The T7 head has an icosahedral shape with an edge of 37.7 +/- 0.5 nm, a volume of (12.0 +/- 1.0) x 10(4) nm3, and a small tail amounting to 6--7% of the head volume. The intraphage DNA region is most probably a hollow sphere. The best fit to the data was obtained with a model in which the hollow sphere filled with a protein core with a diameter of 24 nm. The average degree of swelling (i.e., the ratio of the hydrated to the dry volume) of the particle is 2.3; the degree of swelling of the DNA component is higher, 3.2, and that of the protein part is lower, 1.2.

DNA, Viral↗

Associative phase separation of beta-lactoglobulin/pectin solutions: a kinetic study by small angle static light scattering.

Interpolymer complexation between beta-lactoglobulin (beta-lg) and pectin led to phase separation. Small angle static light scattering and phase contrast microscopy were used to monitor the phase separation of beta-lg/low-methoxyl or high-methoxyl-pectin (LM- or HM-pectin) dispersions as they were slowly acidified from pH 7 to 4 with glucono-delta-lactone (GDL). The monotonic decrease in scattered light intensity with the wave vector was associated with a nucleation and growth phase separation mechanism. Microscopic observations and turbidity measurements showed the increase of complex amounts with lower pH and at higher beta-lg/pectin ratios. The formation of intrapolymer complexes was initiated at pH 6.4 with the LM-pectin and at pH 5.0 with the HM-pectin. Local ordering with increasing amounts of small complexes was observed as scattered light intensity increased at intermediate q values. The beta-lg/LM-pectin complexes at the 5:1 and the 2:1 weight ratios and the beta-lg/HM-pectin complexes at 5:1 weight ratio have fractal structures. The formation of large amounts of small assemblies and sedimentation would be responsible for the decrease in the number and volume mean diameters and fractal dimension of beta-lg/LM-pectin complexes over time.

Kinetics↗

Absence of scaling for the intermediate scattering function of a hard-sphere suspension: static and dynamic x-ray scattering from concentrated polystyrene latex spheres.

X-ray photon correlation spectroscopy and small-angle scattering measurements are presented of the dynamics and structure of concentrated suspensions of charge-stabilized polystyrene latex spheres dispersed in glycerol, for volume fractions from 3% to 52%. The static structures of the suspensions show essentially hard-sphere behavior, and the short-time dynamics shows good agreement with predictions for the wave-vector-dependent collective diffusion coefficient. However, the intermediate scattering function is found to violate a scaling behavior found previously for a sterically stabilized hard-sphere suspension.

Journal Article↗

Detergent organisation in solutions and in crystals of membrane proteins.

The use of neutron scattering in studying the organisation of detergents in pure micelles, in protein/detergent mixed micelles and in crystals of membrane proteins, is reviewed. Small angle scattering has been used to study the size, shape and composition of pure and mixed protein/detergent micelles as well as the effects of adding small amphiphiles. The technique of contrast variation applied to single crystals is described and its application to the determination of the organization of detergent in single crystals of membrane proteins is discussed. A better understanding of protein/detergent interactions should help in producing crystals of membrane proteins more easily as well as clues to the nature of protein/lipid interactions in vivo.

Journal Article↗

Aging in a filled polymer: coherent small angle x-ray and light scattering

Measurements are described using small angle coherent x-ray scattering and small angle dynamic light scattering of motion in fumed silica aggregates suspended in a poly(dimethyl siloxane) melt. At rest, this system develops weakly bound superstructures that are disrupted by mechanical stirring or thermal treatment. The observed relaxation rates correspond to a combination of liquidlike diffusion and a structural relaxation (flocculation) whereby the diffusing silica aggregates recombine into larger agglomerates at long times. Both processes are diffusion controlled. Two samples are investigated. The first, in which the silica is hydrophilic, is a highly viscous liquid for which the respective rate coefficients are about 5x10(-14) cm(2) s(-1) and 2x10(-15) cm(2) s(-1). The second sample, in which the silica surface is hydrophobic, is a thixotropic paste. The same aging mechanism in the diffusion is also observed, but with much slower rate constants, 2x10(-15) cm(2) s(-1) and 9x10(-16) cm(2) s(-1), respectively.

Journal Article↗

Structural model of the 50 S subunit of Escherichia coli ribosomes from solution scattering. I. X-ray synchrotron radiation study.

The application of new methods of small-angle scattering data interpretation to a contrast variation study of the 50 S ribosomal subunit of Escherichia coli in solution is described. The experimental X-ray data from contrast variation with sucrose are analysed in terms of the basic functions in real space and the scattering curves from the volume inaccessible to sucrose and from the regions inside this volume occupied mainly by RNA and by proteins are obtained. From these curves models of the shape of the 50 S subunit and its RNA-rich core are evaluated. These two shapes are positioned so that their difference, which approximates the volume occupied by the proteins, produces a scattering curve which is in good agreement with the scattering from the protein moiety.

Escherichia coli↗

Elasticity effects on domain coarsening of the lamellar-gyroid transition observed in a nonionic surfactant system.

The coarsening process of the gyroid phase of a nonionic surfactant system is investigated by time resolved small angle neutron scattering (SANS) and small angle neutron Laue diffraction techniques. The time evolution of SANS patterns shows anomalous coarsening of the gyroid domains. The observed Laue spot from a gyroid domain becomes elongated along the radial direction with the elapse of time and at a certain time the elongated spot is split into two spots. The results can be interpreted as follows. During the coarsening process, mismatch of the lattice orientation at the domain boundary brings strong stress to the gyroid domain, resulting in the distortion of the domain. The stored stress in the domain finally brings splitting of the gyroid domain. The elastic and fragile nature of the gyroid domains composed of the "soft matter" is responsible for the anomalous coarsening.

Journal Article↗

Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle X-ray scattering.

We have used solution small-angle X-ray scattering to characterize bovine brain calmodulin in the presence and absence of calcium. In the presence of calcium, calmodulin exists in solution as an elongated molecule with a radius of gyration of 21.5 A and a maximum vector length of approximately 62 A. These values are consistent with the dimensions recently determined for the crystal form of rat testis calmodulin. In the absence of calcium, the calmodulin molecule is shorter, the radius of gyration decreases to 20.6 A, and the maximum vector length decreases to approximately 58 A. This change in dimensions is consistent with an overall contraction of the protein through movement of the two lobes closer to each other upon removal of calcium from calmodulin.

Animals↗

A one-dimensional model for small-angle X-ray scattering from crystalline block copolymers.

Small-angle X-ray scattering patterns (SAXS) are widely used to study polymers. Quantitative treatment of the intensity curves is often realized to obtain the long period and the linear crystallinity of semicrystalline homopolymers presenting a lamellar morphology, mainly using the correlation function. But even in the one-dimensional case, block copolymer systems exhibit more complicated morphologies that cannot be fully interpreted by this standard method. In this work, a model has been developed based on a previous treatment applicable to systems characterized by two different densities. Two additional densities have been considered to model four phase systems that can occur with block copolymers (e.g. two different crystalline domains and amorphous parts). The scattering intensity function was derived as a function of various parameters like the number of stacked lamellar units, the mean values and distributions of widths, and the electron densities.

Journal Article↗