The French protein crystallography beamline BM07-FIP2 at the ESRF enables both cryogenic and room-temperature studies on single crystals, with precise control over the deposited X-ray dose thanks to a large, homogeneous top-hat beam. [1] In addition, its sample environment allows for easy integration of the EMBL/ESRF microspectrophotometer [2], enabling in crystallo UV-Visible absorption and...
Protein–inhibitor crystal structures aid medicinal chemists in efficiently improving the potency and selectivity of small-molecule inhibitors. It is estimated that a quarter of lead molecules in drug discovery projects are halogenated. Protein–inhibitor crystal structures have shed light on the role of halogen atoms in ligand binding. They form halogen bonds with protein atoms and improve...
Radiation damage is a faithful attender to X-ray crystallographic studies of metallo-proteins. Thus, care is taken to limit the effects of radiation damage and avoid consequent misinterpretation of X-ray crystallographic results. In our study, we applied defined doses to selectively probe the redox states involved in metal binding.
We studied the cyanobacterial iron binding protein FutA, an...
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Lytic polysaccharide monooxygenases are enzymes [1] binding their active-site copper through the characteristic His-brace motif shown above including two His – one N-terminal – and often also a Tyr. The reaction cycle starts with reduction of the resting state Cu(II) to Cu(I) – in the laboratory usually using ascorbate as small molecule reductant. Despite...
