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temperatures is thought to be from photoelectrons ejected from atoms following the absorption of X-rays. As the photoelectrons traverse the crystal, they lose energy through interactions with atoms in their path resulting in damage. If the X-ray beam is polarized, the photoelectrons are ejected preferentially along the polarization vector. Monte-Carlo simulations [Nave, C., and Hill, M. A. (2005). J Syn. Rad. 12, 299-303] suggest that, when the beam size is only a few microns, most photoelectrons escape the illuminated volume. This leads to the peculiar conclusion that the radiation damage due to photoelectrons may be significantly lower within the illuminated volume than in the volume immediately surrounding the irradiated spot. A second prediction of the calculations is that most of the photoelectron’s energy is abruptly dissipated within the last few microns of its trajectory. Recently, a long focal length Fresnel zone plate was used to provide a focused beam of ~1-micron cross section at the sample position, and high quality diffraction data was obtained from protein crystals. The 15.1 keV, 1-micron beam was used to probe the geometrical distribution and extent of radiation damage in protein crystals. These data confirm that radiation damage is greater along the polarization vector than in the perpendicular direction, radiation damage is maximal 3-4 microns from the center of the beam, and radiation damage does not extend beyond 6 microns.

Towards protein structure determination using two-dimensional crystals and powders