The High Time Resolution Spectrometer (HTRS) aboard the International X-ray Observatory (IXO)

The High Time Resolution Spectrometer (HTRS) is one of the five focal plane instruments of the International X-ray Observatory (IXO). The HTRS is the only instrument matching the top level mission requirement of handling a one Crab X-ray source with an efficiency greater than 10%. It will provide IXO with the capability of observing the brightest X-ray sources of the sky, with sub-millisecond time resolution, low deadtime, low pile-up (less than 2% at 1 Crab), and CCD type energy resolution (goal of 150 eV FWHM at 6 keV). The HTRS is a non-imaging instrument, based on a monolithic array of Silicon Drift Detectors (SDDs) with 31 cells in a circular envelope and a X-ray sensitive volume of 4.5 cm2 x 450 μm. As part of the assessment study carried out by ESA on IXO, the HTRS is currently undergoing a phase A study, led by CNES and CESR. In this paper, we present the current mechanical, thermal and electrical design of the HTRS, and describe the expected performance assessed through Monte Carlo simulations

Anomalous signal from S atoms in protein crystallographic data from an X-ray free-electron laser

X-ray free-electron lasers (FELs) enable crystallographic data collection using extremely bright femtosecond pulses from microscopic crystals beyond the limitations of conventional radiation damage. This diffraction-before-destruction approach requires a new crystal for each FEL shot and, since the crystals cannot be rotated during the X-ray pulse, data collection requires averaging over many different crystals and a Monte Carlo integration of the diffraction intensities, making the accurate determination of structure factors challenging. To investigate whether sufficient accuracy can be attained for the measurement of anomalous signal, a large data set was collected from lysozyme microcrystals at the newly established `multi-purpose spectroscopy/imaging instrument' of the SPring-8 Ångstrom Compact Free-Electron Laser (SACLA) at RIKEN Harima. Anomalous difference density maps calculated from these data demonstrate that serial femtosecond crystallography using a free-electron laser is sufficiently accurate to measure even the very weak anomalous signal of naturally occurring S atoms in a protein at a photon energy of 7.3 keV

Toward unsupervised single-shot diffractive imaging of heterogeneous particles using X-ray free-electron lasers

Single shot diffraction imaging experiments via X-ray free- electron lasers can generate as many as hundreds of thousands of diffraction patterns of scattering objects. Recovering the real space contrast of a scat- tering object from these patterns currently requires a reconstruction process with user guidance in a number of steps, introducing severe bottlenecks in data processing. We present a series of measures that replace user guidance with algorithms that reconstruct contrasts in an unsupervised fashion. We demonstrate the feasibility of automating the reconstruction process by generating hundreds of contrasts obtained from soot particle diffraction experiments

Sensing the wavefront of x-ray free-electron lasers using aerosol spheres

Characterizing intense, focused x-ray free electron laser (FEL) pulses is crucial for their use in diffractive imaging. We describe how the distribution of average phase tilts and intensities on hard x-ray pulses with peak intensities of 10^21 W/cm^2 can be retrieved from an ensemble of diffraction patterns produced by 70 nm-radius polystyrene spheres, in a manner that mimics wavefront sensors. Besides showing that an adaptive geometric correction may be necessary for diffraction data from randomly injected sample sources, our paper demonstrates the possibility of collecting statistics on structured pulses using only the diffraction patterns they generate and highlights the imperative to study its impact on single-particle diffractive imaging