We demonstrate intense emission in the water-window soft x-ray spectral region by controlling the spectral behavior through changing the balance between emissivity and self-absorption in an expanding plasma. The number of photons obtained from a dual laser irradiated target with a 150-ps pre-pulse was maximized at 3.8 × 10 photons/sr in λ = 2.34 - 4.38 nm at a pulse separation time of 7 - 10 ns. Enhancement of the number of photons is attributed to efficient coupling with the main laser pulse while maintaining a tiny source size.
A laser-plasma source emitting photons with energies in the water window spectral range has been used to reveal the radiation chemical yields of single-strand breaks in plasmid DNA as a function of OH radical scavenger concentration. Direct and indirect effects were investigated separately using DNA samples with various levels of hydration. We experimentally determined the value of the efficiency factor for strand cleavage in DNA caused by the reaction with OH radicals at 0.
Time-resolved soft-x-ray-diffraction experiments give access to microscopic processes in a broad range of solid-state materials by probing ultrafast dynamics of ordering phenomena. While laboratory-based high-harmonic generation (HHG) light sources provide the required photon energies, their limited photon flux is distributed over a wide spectral range, rendering typical monochromatic diffraction schemes challenging. Here, we present a scheme for energy-dispersive soft-x-ray diffraction with femtosecond temporal resolution and photon energies across the water window from 200 to 600 eV.
The development of efficient multilayer mirrors for the water window (a spectral region between absorption edges of carbon and oxygen, from 284 to 543 eV) remains a challenge. As the best candidate, the Cr/Sc multilayer provides maximum theoretical reflectivity of about 60% at near-normal incidence around the Sc L absorption edge (397 eV). However, the maximum measured peak reflectance published so far just slightly exceeds 20%.
The recent advances achieved in microscopy technology have led to a significant breakthrough in biological research. Super-resolution fluorescent microscopy now allows us to visualize subcellular structures down to the pin-pointing of the single molecules in them, while modern electron microscopy has opened new possibilities in the study of protein complexes in their native, intracellular environment at near-atomic resolution. Nonetheless, both fluorescent and electron microscopy have remained beset by their principal shortcomings: the reliance on labeling procedures and severe sample volume limitations, respectively.
Correlative microscopy is a powerful technique that combines the advantages of multiple imaging modalities to achieve a comprehensive understanding of investigated samples. For example, fluorescence microscopy provides unique functional contrast by imaging only specifically labeled components, especially in biological samples. However, the achievable structural information on the sample in its full complexity is limited.
