Key research on the coronavirus protein was performed at several beamlines, including the BESSY II synchrotron in Berlin. Additionally, the proteins must be robust enough to undergo exposure to x-rays, or instruments must be fast enough to prevent damage to the fragile proteins from the intense radiation during x-ray diffraction. In order for this method to work on proteins, a sufficient quantity must be synthesized and then crystallized in a highly ordered lattice. When x-rays infringe upon a single-crystal sample, the resulting diffraction pattern can tell researchers the arrangement of atoms within the crystal. One of the prominent methods of protein characterization is x-ray crystallography, which uses x-ray diffraction to provide information about the atomic structure of a crystal. Important new developments would continue to be made in the coming months, and all of these breakthroughs were possible because of both incredible scientists and sophisticated equipment and techniques for protein analysis. By March, a paper had been published describing the structure of the spike protein on the outer surface of the virus. After the initial emergence of COVID-19, caused by the SARS-CoV-2 virus, the genome had already been shared online by early January. We all remember hearing the news of a series of distinct pneumonia infections emerging in Wuhan, China in December 2019 word quickly spread globally, along with this novel coronavirus that seemed similar to the severe acute respiratory syndrome (SARS) virus observed in a 2003 outbreak. So when the COVID-19 pandemic began and scientists around the world scrambled to learn about it as quickly as possible, x-ray diffraction was one of several highly developed methods available to play a large role in their research. Given the vast amount of research done in these fields, it is only natural for them to change and evolve, requiring methods of investigation to evolve alongside them. X-ray diffraction has been used in the medical and pharmaceutical industry for decades.
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