Tables for
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

International Tables for Crystallography (2006). Vol. F, ch. 6.1, p. 129   | 1 | 2 |

Section Cross fire

U. W. Arndta

aLaboratory of Molecular Biology, Medical Research Council, Hills Road, Cambridge CB2 2QH, England Cross fire

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The cross fire is defined as the angle or the half-angle between extreme rays in the beam incident on a given point of the sample. In the absence of focusing elements, such as specularly reflecting mirrors, the X-ray beam diverges from the source. A diverging beam can be turned into a converging one by reflection from a curved mirror or crystal. A crystal with constant lattice spacing can change the sign, but not the magnitude, of the angle between rays, whatever the curvature of the crystal; the deviation produced by a reflection anywhere on the surface of the crystal must always be twice the Bragg angle. It is possible to change a divergent beam into a convergent one with a different cross fire by specular reflection at a mirror or by means of a crystal in which the lattice spacing varies from point to point along the length of the plate. Such variable-spacing reflectors may be either artificial-crystal multilayers (Schuster & Göbel, 1997[link]) or, less commonly, natural crystals whose spacing is modified by variable doping or by a temperature gradient along the crystal plate (Smither, 1982[link]). In the neutron-scattering community, graded-spacing multilayer monochromators are usually referred to as `supermirrors' (see Section in Chapter 6.2[link] ).

The construction of curved mirrors and curved-crystal monochromators is discussed below.

As a general rule, the better the collimation of the incident X-ray beam, that is, the smaller the cross fire and the more nearly parallel the beam, the cleaner the diffraction pattern and the lower the background. Synchrotron-radiation sources permit a certain prodigality in X-ray intensity and the beams from them are thus usually better collimated than beams from conventional sources.

The useful degree of collimation depends on the crystal under investigation. The aim in the design of an instrument for data collection from single crystals must be to make the widths of the angular profiles of the reflection small, but these widths cannot be reduced beyond the rocking-curve width determined by the mosaic spread of the sample, however small the cross fire. The mosaic spread of a typical protein crystal is often quoted as being about 10−3 rad or about 3.4 minutes of arc. However, there are many crystals with much larger mosaicities; for such samples, the intensity of the X-ray beam, expressed as the total number of photons which strike the crystal, can be increased by permitting a larger cross fire.

The mosaic spread must be understood as the angle between individual domains of the mosaic crystal. These domains may be as large as 100 µm, that is, they may have dimensions not so very much smaller than those of the macroscopic crystal. The individual rocking-curve widths may be as small as 10 seconds of arc (50 µrad). Fourme et al. (1995[link]) have discussed the implications of this degree of perfection if the collimation is improved to a stage where it can be exploited.

The way in which the cross fire influences the angular widths of the reflections depends on the instrument geometry. In a single-counter four-circle diffractometer, all reflections are brought onto the equator and the crystal is rotated about an axis perpendicular to the equatorial plane. The cross fire should, therefore, be small parallel to the equatorial plane, i.e. usually in the horizontal plane. The cross fire in the plane containing the rotation axis affects the angular width of the reflections much less, and it could thus be made larger in the interest of a high intensity.

The situation is different if the diffractometer is fitted with an electronic area detector, such as a CCD or other TV detector or a multi-wire proportional chamber (see Part 7[link] ). Here, the widths of reflections in upper levels are affected by the cross fire in the plane containing the crystal rotation axis, and the divergence or convergence of the beam in this plane should also be kept small.

With recording on photographic film or image plates, each exposure, or `shot' or `frame', corresponds to a crystal rotation that is usually many times larger than the angular width of a reflection. It is then less important to keep the cross fire small in the plane perpendicular to the rotation axis of the crystal.

In many collimation arrangements, the cross fire can be chosen independently in the two planes. In the absence of monochromators or mirrors, the cross fire is determined by beam apertures, which can be rectangular slits; it is, of course, simpler to employ circular holes, which give the same cross fire in both planes.


Fourme, R., Ducruix, A., Ries-Kautt, M. & Capelle, B. (1995). The perfection of protein crystals probed by direct recording of Bragg reflection profiles with a quasi-planar X-ray wave. J. Synchrotron Rad. 2, 136–142.
Schuster, M. & Göbel, H. (1997). Application of graded multi-layer optics in X-ray diffraction. Adv. X-ray Anal. 39, 57–71.
Smither, R. K. (1982). New methods for focusing X-rays and gamma rays. Rev. Sci. Instrum. 53, 131–141.

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