4000th protein structure decoded at BESSY II
The 4000th protein structure from HZB BESSY published in PDB shows the G64S variant of FKBP51 in complex with the highly selective ligand SAFit (marked structure). © C. Meyners/TU Darmstadt/HZB
The 4000th structure is the molecule FKBP51, which is linked to stress-induced diseases such as depression, chronic pain and diabetes. The team led by Prof. Felix Hausch, TU Darmstadt, is using the knowledge of the three-dimensional structure to develop new strategies for the design of suitable drugs.
Many diseases are related to malfunctions of proteins in the organism. The three-dimensional architecture of these molecules is often extremely complex, but provides valuable clues as to how the malfunction could be remedied, for example by drugs that bind perfectly into a "pocket" on the target molecule and block the malfunction. The structure of proteins can be deciphered with X-ray analyses at the MX beamlines of BESSY II.
The 4000th structure from BESSY II has now been entered in the Protein Data Bank (www.rcsb.org/pdb), which contains all experimentally determined protein structures. The team led by Prof. Felix Hausch from TU Darmstadt had produced protein crystals from the molecule FKBP51 and examined them on the MX beamlines.
This is a protein that plays a special role in major health problems of our time. FKBP51 regulates the signal transduction of steroid hormone receptors, which can be disturbed by stress. This can trigger depression, chronic pain or diseases such as diabetes and obesity. The protein FKBP51 has shown promise as a target for drugs against these diseases. "Protein structure analysis shows us where interesting "pockets" are located in the molecule that could be drug targets," says Dr. Christian Meyners from the TU Darmstadt team.
High-energy X-rays leave a trace of destruction in bone collagen
A team of medical researchers at Charité has analyzed damage by focused high energetic X-rays in bone samples from fish and mammals at BESSY II. With a combination of microscopy techniques, the scientists could document the destruction of collagen fibres induced by electrons emitted from the mineral crystals. X-ray methods might impact bone samples when measured for a long time they conclude.
Neutron experiments reveal what maintains bones in good function
What keeps bones able to remodel themselves and stay healthy? A team from Charité Berlin has discovered clues to the key function of non-collagen protein compounds and how they help bone cells react to external load. The scientists used fish models to examine bone samples with and without bone cells to elucidate differences in microstructures and the incorporation of water. Using 3D neutron tomography at the Berlin research reactor BER II, they succeeded for the first time in precisely measuring the water diffusion across bone material - with a surprising result.
New monochromator optics for tender X-rays
Until now, it has been extremely tedious to perform measurements with high sensitivity and high spatial resolution using X-ray light in the tender energy range of 1.5 - 5.0 keV. Yet this X-ray light is ideal for investigating energy materials such as batteries or catalysts, but also biological systems. A team from HZB has now solved this problem: The newly developed monochromator optics increase the photon flux in the tender energy range by a factor of 100 and thus enable highly precise measurements of nanostructured systems. The method was successfully tested for the first time on catalytically active nanoparticles and microchips.