Publications by authors named "Pradervand C"

The upgrade of the Swiss Light Source, called SLS 2.0, necessitates comprehensive updates to all 18 user front ends. This upgrade is driven by the increased power of the synchrotron beam, reduced floor space, changing source points, new safety regulations and enhanced beam properties, including a brightness increase by up to a factor of 40.

View Article and Find Full Text PDF
Article Synopsis
  • The researchers introduced a new resonant inelastic hard x-ray scattering setup at the Bernina beamline in SwissFEL, featuring high energy, momentum, and temporal resolution using a compact Johann-type spectrometer.
  • They achieved an approximate resolution of 180 meV while studying honeycomb iridate α-LiIrO, confirming that their findings align well with previous synchrotron data.
  • The time-resolved RIXS transients revealed energy loss changes less than 2 eV, linked to electron hopping in the lattice, which were attributed to modulation of inter-site transition scattering efficiency and transient changes in on-site Coulomb interaction.
View Article and Find Full Text PDF

Gas attenuators are important devices providing accurate variation of photon intensity for soft X-ray beamlines. In the SwissFEL ATHOS beamline front-end the space is very limited and an innovative approach has been taken to provide attenuation of three orders of magnitude up to an energy of 1200 eV. Additive manufacturing of a differential pumping system vacuum manifold allowed a triple pumping stage to be realized in a space of less than half a meter.

View Article and Find Full Text PDF

The SwissFEL soft X-ray free-electron laser (FEL) beamline Athos will be ready for user operation in 2021. Its design includes a novel layout of alternating magnetic chicanes and short undulator segments. Together with the APPLE X architecture of undulators, the Athos branch can be operated in different modes producing FEL beams with unique characteristics ranging from attosecond pulse length to high-power modes.

View Article and Find Full Text PDF

The list of authors in the paper by Juranić et al. (2018) [J. Synchrotron Rad.

View Article and Find Full Text PDF

The extension of transient grating spectroscopy to the x-ray regime will create numerous opportunities, ranging from the study of thermal transport in the ballistic regime to charge, spin, and energy transfer processes with atomic spatial and femtosecond temporal resolution. Studies involving complicated split-and-delay lines have not yet been successful in achieving this goal. Here we propose a novel, simple method based on the Talbot effect for converging beams, which can easily be implemented at current x-ray free electron lasers.

View Article and Find Full Text PDF

In this work, the performance of thin silicon carbide membranes as material for radiation hard X-ray beam position monitors (XBPMs) is investigated. Thermal and electrical behavior of XBPMs made from thin silicon carbide membranes and single-crystal diamond is compared using finite-element simulations. Fabricated silicon carbide devices are also compared with a 12 µm commercial polycrystalline diamond XBPM at the Swiss Light Source at the Paul Scherrer Institute.

View Article and Find Full Text PDF

The SwissFEL Aramis beamline, covering the photon energies between 1.77 keV and 12.7 keV, features a suite of online photon diagnostics tools to help both users and FEL operators in analysing data and optimizing experimental and beamline performance.

View Article and Find Full Text PDF

The two-color operation of free electron laser (FEL) facilities allows the delivery of two FEL pulses with different energies, which opens new possibilities for user experiments. Measuring the arrival time of both FEL pulses relative to the external experimental laser and to each other improves the temporal resolution of the experiments using the two-color FEL beam and helps to monitor the performance of the machine itself. This work reports on the first simultaneous measurement of the arrival times of two hard X-ray FEL pulses with the THz streak camera.

View Article and Find Full Text PDF

The Parallel Robotics Inspired Goniometer (PRIGo) is a novel compact and high-precision goniometer providing an alternative to (mini-)kappa, traditional three-circle goniometers and Eulerian cradles used for sample reorientation in macromolecular crystallography. Based on a combination of serial and parallel kinematics, PRIGo emulates an arc. It is mounted on an air-bearing stage for rotation around ω and consists of four linear positioners working synchronously to achieve x, y, z translations and χ rotation (0-90°), followed by a ϕ stage (0-360°) for rotation around the sample holder axis.

View Article and Find Full Text PDF

The accurate measurement of the arrival time of a hard X-ray free electron laser (FEL) pulse with respect to a laser is of utmost importance for pump-probe experiments proposed or carried out at FEL facilities around the world. This manuscript presents the latest device to meet this challenge, a THz streak camera using Xe gas clusters, capable of pulse arrival time measurements with an estimated accuracy of several femtoseconds. An experiment performed at SACLA demonstrates the performance of the device at photon energies between 5 and 10 keV with variable photon beam parameters.

View Article and Find Full Text PDF

A new diffractometer for microcrystallography has been developed for the three macromolecular crystallography beamlines of the Swiss Light Source. Building upon and critically extending previous developments realised for the high-resolution endstations of the two undulator beamlines X06SA and X10SA, as well as the super-bend dipole beamline X06DA, the new diffractometer was designed to the following core design goals. (i) Redesign of the goniometer to a sub-micrometer peak-to-peak cylinder of confusion for the horizontal single axis.

View Article and Find Full Text PDF

Automatic loop centring has been developed as part of the automation process in crystallographic data collection at the Swiss Light Source. The procedure described here consists of an optional set-up part, in which the background images are taken, and the actual centring part. The algorithm uses boundary and centre-of-mass detection at two different microscope image magnifications.

View Article and Find Full Text PDF

The cryocooling of protein crystals to temperatures of around 100 K drastically reduces X-ray-induced radiation damage. The majority of macromolecular data collection is therefore performed at 100 K, yielding diffraction data of higher resolution and allowing structure determination from much smaller crystals. However, at third-generation synchrotron sources radiation damage at 100 K still limits the useful data obtainable from a crystal.

View Article and Find Full Text PDF

A time-resolved Laue X-ray diffraction technique has been used to explore protein relaxation and ligand migration at room temperature following photolysis of a single crystal of carbon monoxymyoglobin. The CO ligand is photodissociated by a 7.5 ns laser pulse, and the subsequent structural changes are probed by 150 ps or 1 micros X-ray pulses at 14 laser/X-ray delay times, ranging from 1 ns to 1.

View Article and Find Full Text PDF
Article Synopsis
  • The bacterial blue-light photoreceptor, photoactive yellow protein, undergoes structural changes when stimulated by a brief laser pulse, observable in real time using advanced X-ray diffraction techniques.
  • A key event in the photocycle is the flipping of a carbonyl group in the chromophore, which significantly influences the protein's behavior rather than the expected isomerization of the double bond.
  • This carbonyl group movement causes a ripple effect, described as a "protein quake," that spreads throughout the entire protein structure, illustrating how light-induced changes can propagate at a molecular level.
View Article and Find Full Text PDF

Photoactive yellow protein (PYP) is a member of the xanthopsin family of eubacterial blue-light photoreceptors. On absorption of light, PYP enters a photocycle that ultimately transduces the energy contained in a light signal into an altered biological response. Nanosecond time-resolved x-ray crystallography was used to determine the structure of the short-lived, red-shifted, intermediate state denoted [pR], which develops within 1 nanosecond after photoelectronic excitation of the chromophore of PYP by absorption of light.

View Article and Find Full Text PDF

The blue-light photoreceptor photoactive yellow protein (PYP) undergoes a self-contained light cycle. The atomic structure of the bleached signaling intermediate in the light cycle of PYP was determined by millisecond time-resolved, multiwavelength Laue crystallography and simultaneous optical spectroscopy. Light-induced trans-to-cis isomerization of the 4-hydroxycinnamyl chromophore and coupled protein rearrangements produce a new set of active-site hydrogen bonds.

View Article and Find Full Text PDF

The biological activity of macromolecules is accompanied by rapid structural changes. The photosensitivity of the carbon monoxide complex of myoglobin was used at the European Synchrotron Radiation Facility to obtain pulsed, Laue x-ray diffraction data with nanosecond time resolution during the process of heme and protein relaxation after carbon monoxide photodissociation and during rebinding. These time-resolved experiments reveal the structures of myoglobin photoproducts, provide a structural foundation to spectroscopic results and molecular dynamics calculations, and demonstrate that time-resolved macromolecular crystallography can elucidate the structural bases of biochemical mechanisms on the nanosecond time scale.

View Article and Find Full Text PDF

Laue diffraction patterns with an exposure time of ca 60 ps have been acquired at the European Synchrotron Radiation Facility (ESRF) on protein crystals by using the single-bunch mode of the storage ring. A 10 ns laser pulse initiating photodissociation was synchronized with the X-ray pulse. The potential for a quantitative detection of conformational changes in proteins on the nanosecond timescale with this technique is demonstrated using the example of carbonmonoxymyoglobin, from simulations and real data.

View Article and Find Full Text PDF