Sample damage by X-rays and other radiation limits the resolution of structural studies on non-repetitive and non-reproducible structures such as individual biomolecules or cells. Cooling can slow sample deterioration, but cannot eliminate damage-induced sample movement during the time needed for conventional measurements. Analyses of the dynamics of damage formation suggest that the conventional damage barrier (about 200 X-ray photons per A2 with X-rays of 12 keV energy or 1 A wavelength) may be extended at very high dose rates and very short exposure times. Here we have used computer simulations to investigate the structural information that can be recovered from the scattering of intense femtosecond X-ray pulses by single protein molecules and small assemblies. Estimations of radiation damage as a function of photon energy, pulse length, integrated pulse intensity and sample size show that experiments using very high X-ray dose rates and ultrashort exposures may provide useful structural information before radiation damage destroys the sample. We predict that such ultrashort, high-intensity X-ray pulses from free-electron lasers that are currently under development, in combination with container-free sample handling methods based on spraying techniques, will provide a new approach to structural determinations with X-rays.

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Synchrotron radiation (SR) is having a very large impact on interdisciplinary science and has been tremendously successful with the arrival of third generation synchrotron x-ray sources. But the revolution in x-ray science is still gaining momentum. Even though new storage rings are currently under construction, even more advanced rings are under design (PETRA III and the ultra high energy x-ray source) and the uses of linacs (energy recovery linac, x-ray free electron laser) can take us further into the future, to provide the unique synchrotron light that is so highly prized for today's studies in science in such fields as materials science, physics, chemistry and biology, for example. All these machines are highly reliant upon the consequences of Einstein's special theory of relativity. The consequences of relativity account for the small opening angle of synchrotron radiation in the forward direction and the increasing mass an electron gains as it is accelerated to high energy. These are familiar results to every synchrotron scientist. In this paper we outline not only the origins of SR but discuss how Einstein's strong character and his intuition and excellence have not only marked the physics of the 20th century but provide the foundation for continuing accelerator developments into the 21st century.

We have carried out a ptychographic scanning coherent diffraction imaging experiment on a test object in order to characterize the hard x-ray nanobeam in a scanning x-ray microscope. In addition to a high resolution image of the test object, a detailed quantitative picture of the complex wave field in the nanofocus is obtained with high spatial resolution and dynamic range. Both are the result of high statistics due to the large number of diffraction patterns. The method yields a complete description of the focus, is robust against inaccuracies in sample positioning, and requires no particular shape or prior knowledge of the test object.

At low emittance synchrotron sources it has become possible to perform structure determinations from the measurement of multiple microcrystals which were previously considered too small for diffraction experiments. Conventional mounting techniques do not fulfill the requirements of these new experiments. They significantly contribute to background scattering and it is difficult to locate the crystals, making them incompatible with automated serial crystallography. We have developed a micro-fabricated sample holder from single crystalline silicon with micropores, which carries up to thousands of crystals and significantly reduces the background scattering level. For loading, the suspended microcrystals are pipetted onto the chip and excess mother liquor is subsequently soaked off through the micropores. Crystals larger than the pore size are retained and arrange themselves according to the micropore pattern. Using our chip we were able to collect 1.5 Å high resolution diffraction data from protein microcrystals with sizes of 4 micrometers and smaller.