X-ray monochromatization

Fig. 2.3. Schematic diagram of X-ray monochromatization to remove satellites, eliminate bremsstrahlung background and separate the Al Ko i,2 doublet. Courtesy of Kratos Analytical.

An X-ray powder photograph taken with a focusing camera and X rays monochromatized by crystal reflection would probably show more than 100 powder lines, providing a more rigorous text of the proposed structure. Accurate values of predicted intensities of the lines will become available only after coordinates have been assigned to all of the atoms, a formidable task with such a complicated structure. This task is now being attempted (S. Samson, personal communication). 

Figure 18 X-ray monochromatic Laue pattern of TTF-TCNQ at 110 K. The horizontal direction is parallel to the one-dimensional i7-axis. (Reproduced from J. R Pouget et al., Rhys. Rev. Letters, 37 (1976) 437, Fig. 1(a))...

Fig. 5.18. An ESCA instrument with X-ray monochromatization and dispersion compensation...

A further advantage occurring from X-ray monochromatization is the removal of satellites (Kaa K3 etc.) and bremsstrahlen (white radiation) leading to clearer cut spectra with much improved signal/ background. 

X-ray spectrometer An apparatus used in the X-ray study of crystals in which a fine beam of monochromatic X-rays impinges at a measured angle on the face of a crystal mounted in its path, and in which the intensity of the X-rays diffracted in various directions by the crystal is measured with an ionization chamber mounted on an arm of the spectrometer table, or is recorded photographically. 

A much better way would be to use phase contrast, rather than attenuation contrast, since the phase change, due to changes in index of refraction, can be up to 1000 times larger than the change in amplitude. However, phase contrast techniques require the disposal of monochromatic X-ray sources, such as synchrotrons, combined with special optics, such as double crystal monochromatics and interferometers [2]. Recently [3] it has been shown that one can also obtain phase contrast by using a polychromatic X-ray source provided the source size and detector resolution are small enough to maintain sufficient spatial coherence. 

Figure 8.14 The monochromatized AlATa carbon Is X-ray photoelectron spectrum of ethyltrifluoroacetate showing the chemical shifts relative to an ionization energy of 291.2 eV (Reproduced, with permission, from Gelius, U., Basilier, E., Svensson, S., Bergmark, T. and Siegbahn, K., J. Electron Spectrosc., 2, 405, 1974)...

If monochromatic X-rays are used as the ionizing radiation the experimental technique is very similar to that for XPS (Section 8.1.1) except that it is the kinetic energy of the Auger electrons which is to be measured. Alternatively, a monochromatic electron beam may be used to eject an electron. The energy E of an electron in such a beam is given by... 

Step 2. The computer opens a shutter, bathing the crystal in a monochromatic x-ray beam. The computer rotates the crystal for about one minute and the rotation diffraction image is stored on the detector and then read into the computer memory. When the operator examines the image and is confident that the sample is indeed a single crystal, the experiment can proceed. 

A very narrow window produces monochromatic radiation that is still several orders of magnitude more intense than the beam from conventional rotating anode x-ray sources. Sucb beams allow crystallographers to record diffraction patterns from very small crystals of the order of 50 micrometers or smaller. In addition, the diffraction pattern extends to higher resolution and consequently more accurate structural details are obtained as described later in this chapter. The availability and use of such beams have increased enormously in recent years and have greatly facilitated the x-ray determination of protein structures. 

Figure 18.5 Schematic view of a diffraction experiment, (a) A narrow beam of x-rays (red) is taken out from the x-ray source through a collimating device. When the primary beam hits the crystal, most of it passes straight through, but some is diffracted by the crystal. These diffracted beams, which leave the crystal in many different directions, are recorded on a detector, either a piece of x-ray film or an area detector, (b) A diffraction pattern from a crystal of the enzyme RuBisCo using monochromatic radiation (compare with Figure 18.2b, the pattern using polychromatic radiation). The crystal was rotated one degree while this pattern was recorded.

Figure 18.8 Two diffracted beams (purple and orange), each of which is defined by three properties amplitude, which is a measure of the strength of the beam and which is proportional to the intensity of the recorded spot phase, which is related to its interference, positive or negative, with other beams and wavelength, which is set by the x-ray source for monochromatic radiation.

Several different techniques are used to study the structure of protein molecules Protein crystals are difficult to grow X-ray sources are either monochromatic or polychromatic... 

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