LiXEdrom: Innovative measuring chamber for X-ray study of liquid jets

Close-up of the liquid-jet.

Close-up of the liquid-jet.

Schematic drawing of the LiXEdrom setup for X-ray <br /> absorption and X-ray emission <br /> spectroscopy on the liquid-jet

Schematic drawing of the LiXEdrom setup for X-ray
absorption and X-ray emission
spectroscopy on the liquid-jet

Until now, the only way to study liquids by soft X-ray emission spectroscopy (XES) has been through a membrane window. Now, researchers of Helmholtz-Zentrum Berlin have carried out an XES study of a free micro-liquid jet on the synchrotron.

X-rays are the medium of choice for many scientific studies. When you shine them on a sample, they literally shed light on the material’s structure, providing loads of information about it. Unfortunately, this mostly applies to solids only, since the sample has to be in a vacuum for the entire time it is being irradiated with soft X-rays. For liquids, that means you have to remove all the water. In the case of biological samples such as proteins, however, this destroys their natural environment. The solution to this problems has always been to measure liquids through membranes. These membranes keep the evacuated side separate from the non-evacuated side. The trouble is, one can never really be sure whether or not membrane effects are distorting the measurement results.

At Helmholtz-Zentrum Berlin (HZB), Emad Aziz, head of a junior research group, has shown that liquids can be investigated by X-ray emission spectroscopy without using membranes after all. At the synchrotron source BESSY II, the group has built a special setup – the LiXEdrom. It is unique in that the liquid is shot as a jet through the X-ray beam. The jet from the nozzle becomes so thin and, at 80 metres per second, so fast that the vacuum can be maintained without the need of a membrane.

“On our LiXEdrom, we create a vacuum in the liquid chamber of up to 10-6 millibar, and can now perform both absorption and emission measurements, giving us even more precise information about the structure of a material,” says Emad Aziz. It also allows a clear “view” of elements that possess absorption and emission energies similar to the energies of the membrane materials, and would therefore overlap with the membrane in the spectrum when measured. This concerns above all carbon and nitrogen – precisely those elements of interest in biological samples.

In their first measurements, published in Chemical Physics (DOI: 10.1016/JChemPhys.2010.08.023) and selected for the cover, the group demonstrated they can achieve energy resolutions on their LiXEdrom comparable to those of the latest high resolution XES spectrometers. For water, they have proven that results obtained from an earlier setup were not overlapped by disturbing membrane effects. They have also studied the electronic structure of nickel ions, unhampered by a risk of deposits on a membrane wall distorting the results. For many applications such as protein studies, this is a significant step towards obtaining reliable structural information.

Original paper in Chem. Phys., DOI 10.1016/JChemPhys.2010.08.023
„High Resolution X-ray Emission Spectroscopy of Water and Aqueous Ions Using the Micro-Jet Technique”, K.M. Lange et al.

IH

  • Copy link

You might also be interested in

  • Protein crystallography at BESSY II: faster, better and more and more automatic
    Interview
    04.03.2026
    Protein crystallography at BESSY II: faster, better and more and more automatic
    Many diseases are linked to malfunctions of proteins in the organism. The three-dimensional architecture of these molecules is often highly complex, but it can provide valuable insights into biological processes and the development of drugs. X-ray diffraction at the MX beamlines of BESSY II can be used to decipher the 3D structure of proteins. To date, more than 5000 structures have been solved at the three MX beamlines. Here, we present a review and an outlook with  Manfred Weiss, head of the research group for macromolecular crystallography. 
  • 5000th protein structure at BESSY II: Starting point for a COVID drug
    Science Highlight
    26.02.2026
    5000th protein structure at BESSY II: Starting point for a COVID drug
    Many proteins have a complex architecture that enables biological functions. Molecules can bind to specific sites on a protein and alter its function. A team at HZB has now investigated the Nsp1 protein, which plays a role in infection with the SARS-CoV-2 virus. They analysed protein crystals, previously mixed with molecules from a fragment library, and discovered a total of 21 candidates as starting points for drug development. At the same time, they also decoded the 5000th structure at BESSY II.
  • What Zinc concentration in teeth reveals
    Science Highlight
    19.02.2026
    What Zinc concentration in teeth reveals
    Teeth are composites of mineral and protein, with a bulk of bony dentin that is highly porous. This structure is allows teeth to be both strong and sensitive. Besides calcium and phosphate, teeth contain trace elements such as zinc. Using complementary microscopy imaging techniques, a team from Charité Berlin, TU Berlin and HZB has quantified the distribution of natural zinc along and across teeth in 3 dimensions. The team found that, as porosity in dentine increases towards the pulp, zinc concentration increases 5~10 fold. These results help to understand the influence of widely-used zinc-containing biomaterials (e.g. filling) and could inspire improvements in dental medicine.