After more than half a century of evolution, machine learning and artificial intelligence, in general, are entering truly exciting era broad application commercial research sectors. In X-ray crystallography, its to structural biology, is finding home within expert automated systems, forecasting experiment data analysis outcomes, predicting whether crystals can be grown even generating macromole...

In 1912, Max von Laue and collaborators first observed diffraction spots from a millimeter-sized crystal of copper sulfate using an Xray tube. Crystallography was born of this experiment, and since then, diffraction by both X-rays and electrons has revealed a myriad of inorganic and organic structures, including structures of complex protein assemblies. Advancements in X-ray sources have spurre...

X-ray crystallography and NMR spectroscopy provide the only sources of experimental data from which protein structures can be analyzed at high or even atomic resolution. The degree to which these methods complement each other as sources of structural knowledge is a matter of debate; it is often proposed that small proteins yielding high quality, readily analyzed NMR spectra are a subset of thos...

In modern life science research, structural information on proteins is indispensable for understanding the mechanisms of their biological functions. Many protein structures have been determined by X-ray crystallography, which has developed in conjunction with molecular biology experiments and synchrotron radiation development. Since Nobel Prize Chemistry 2017, rapid progress cryo-EM hardware an...

Structural information of the different conformational states of the two prototypical light-sensitive membrane proteins, bacteriorhodopsin and rhodopsin, has been obtained in the past by X-ray cryo-crystallography and cryo-electron microscopy. However, these methods do not allow for the structure determination of most intermediate conformations. Recently, the potential of X-Ray Free Electron La...