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Coherent X-rays (coherent + x-ray)
Selected AbstractsDetection and characterization of ultra-thin films with neutron reflectometryACTA CRYSTALLOGRAPHICA SECTION A, Issue 1 2009Z. Tun Specular reflectometry, being a technique based on interference between coherent X-ray or neutron beams, is considered to have a fundamental limit in sensing the presence of films that are too thin for the maximum momentum transfer, Qmax, to which reflectivity has been measured. However, it is known both experimentally and from simulations that an ultra-thin film, with thickness t << 2,/Qmax, can be detected if it exists sandwiched between two contrast-matched media. This possibility is qualitatively explained using phase-vector diagrams. The diagrams also show that the detection is through unmistakable shifts of the interference maxima and minima, and that the scattering-length density of the ultra-thin film determined by least-squares analysis is unique. [source] Grazing-incidence scattering of coherent X-rays from a liquid surfaceJOURNAL OF SYNCHROTRON RADIATION, Issue 6 2005Anders Madsen The scattering image produced by coherent X-rays appears grainy and is denoted a speckle pattern. An analysis of the static and time-dependent properties of a speckle pattern generated by scattering of a partially coherent synchrotron beam from a liquid surface is given here. Unique surface sensitivity is achieved by applying the X-rays under a grazing angle of incidence. The observed contrast of the speckle pattern depends on the momentum transfer parallel to the surface, unlike the case of transmission small-angle X-ray scattering (SAXS), where essentially no dependence of the contrast has been observed. The appearance of the speckles and the contrast of the image can be understood qualitatively by use of geometrical arguments and by the fact that liquid surfaces are extremely flat. [source] Overview and new developments in softer X-ray (2Å < , < 5Å) protein crystallographyJOURNAL OF SYNCHROTRON RADIATION, Issue 1 2004John R. Helliwell New methodologies with synchrotron radiation and X-ray free electron lasers (XFELs) in structural biology are being developed. Recent trends in harnessing softer X-rays in protein crystallography for phase determination are described. These include reference to a data-collection test at 2.6 Å wavelength with a lysozyme crystal on SRS station 7.2 (Helliwell, 1983) and also use of softer X-rays (2,Å wavelength) to optimise f," at the xenon L1 absorption edge in the Single Isomorphous Replacement Optimised Anomalous Scattering ('SIROAS') structure determination of apocrustacyanin A1 with four, partially occupied, xenon atoms (Cianci et al., 2001; Chayen et al., 2000). The hand of the protein was determined using the f," enhanced sulphur anomalous signal from six disulphides in the protein dimer of 40,kDa. In a follow-up study the single wavelength xenon L1 -edge f," optimised data set alone was used for phase determination and phase improvement by solvent flattening etc. (CCP4 DM) (Olczak et al., 2003). Auto-tracing of the protein was feasible but required additional diffraction data at higher resolution. This latter could be avoided in future by using improved tilted detector settings during use of softer X-rays, i.e. towards back-scattering recording (Helliwell, 2002). The Olczak et al. study has already led to optimisation of the new SRS beamline MPW,MAD,10 (see www.nwsgc.ac.uk) firstly involving the thinning of the beryllium windows as much as possible and planning for a MAR Research tilted detector `desk top beamline' geometry. Thus the use of softer, i.e. 2 to 3,Å wavelength range, X-rays will allow optimisation of xenon and iodine L -edge f," and enhancing of sulphur f," signals for higher throughput protein crystallography. Softer X-rays utilisation in protein crystallography includes work done on SRS bending-magnet station 7.2 in the early 1980s by the author as station scientist (Helliwell, 1984). In the future development of XFELs these softer X-ray wavelengths could also be harnessed and relax the demands to some extent on the complexity and cost of an XFEL. Thus, by use of say 4,Å XFEL radiation and use of a back-scattering geometry area detector the single molecule molecular transform could be sampled to a spatial resolution of 2,Å, sufficient, in principle, for protein model refinement (Miao et al., 1999). Meanwhile, Miao et al. (2003) report the first experimental recording of the diffraction pattern from intact Escherichia coli bacteria using coherent X-rays, with a wavelength of 2,Å, at a resolution of 30,nm and a real-space image constructed. The new single-particle X-ray diffraction-imaging era has commenced. [source] Phase imaging using highly coherent X-rays: radiography, tomography, diffraction topographyJOURNAL OF SYNCHROTRON RADIATION, Issue 3 2000José Baruchel Several hard X-rays imaging techniques greatly benefit from the coherence of the beams delivered by the modern synchrotron radiation sources. This is illustrated with examples recorded on the `long' (145,m) ID19 `imaging' beamline of the ESRF. Phase imaging is directly related to the small angular size of the source as seen from one point of the sample (`effective divergence' , microradians). When using the `propagation' technique, phase radiography and tomography are instrumentally very simple. They are often used in the `edge detection' regime, where the jumps of density are clearly observed. The in situ damage assessment of micro-heterogeneous materials is one example of the many applications. Recently a more quantitative approach has been developed, which provides a three-dimensional density mapping of the sample (`holotomography'). The combination of diffraction topography and phase-contrast imaging constitutes a powerful tool. The observation of holes of discrete sizes in quasicrystals, and the investigation of poled ferroelectric materials, result from this combination [source] Diffraction and imaging study of imperfections of crystallized lysozyme with coherent X-raysACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2004Z. W. Hu Phase-contrast X-ray diffraction imaging and high-angular-resolution diffraction combined with phase-contrast radiographic imaging were employed to characterize defects and perfection of a uniformly grown tetragonal lysozyme crystal in the symmetric Laue case. The full-width at half-maximum (FWHM) of a 4,4,0 rocking curve measured from the original crystal was ,16.7,arcsec and imperfections including line defects, inclusions and other microdefects were observed in the diffraction images of the crystal. The observed line defects carry distinct dislocation features running approximately along the ,1,1,0, growth front and have been found to originate mostly in a central growth area and occasionally in outer growth regions. Inclusions of impurities or formations of foreign particles in the central growth region are resolved in the images with high sensitivity to defects. Slow dehydration led to the broadening of a fairly symmetric 4,4,0 rocking curve by a factor of ,2.6, which was primarily attributed to the dehydration-induced microscopic effects that are clearly shown in X-ray diffraction images. The details of the observed defects and the significant change in the revealed microstructures with drying provide insight into the nature of imperfections, nucleation and growth, and the properties of protein crystals. [source] | ||||||||||