First report on the application of synchrotron radiation to protein crystallography. Order of authorship in the original publication: Phillips, Wlodwawer..., Hodgson. Digital facsimile from pnas.org at this link.

"Synchrotrons can now produce X-rays that are one trillion times brighter than the X-rays Rosalind Franklin used for Photo 51, according to University of Liverpool biophysicist Samar Hasnain, editor in chief of the Journal of Synchrotron Radiation and other journals of the International Union of Crystallography. Indeed, synchrotrons have vastly expanded the scope and refinement of investigations of biological structures and dynamics. They have enabled dazzling biological discoveries, including those associated with five Nobel Prizes in the past 20 years. The most recent of these were Brian Walker [i.e Brian Kobilka] and Robert Lefkowitz's 2012 Nobel Prize in Chemistry for their work on G protein–coupled receptors, membrane proteins that send signals of extracellular molecules to the cell's interior, and Thomas Steitz, Venki Ramakrishnan, and Ada Yonath's 2009 Nobel Prize in Chemistry for their work on the structure of the ribosome, the cell's organelle for synthesizing proteins for many purposes. Walker [i.e. Brian Kobilka] and Lefkowitz's synchrotron work was primarily done at the Advanced Photon Source (APS) synchrotron at Argonne National Laboratory, in Illinois, and the Steitz, Ramakrishnan, and Yonath ribosome work involved research at multiple synchrotrons, including APS and the European Synchrotron Radiation Facility (ESRF), in Grenoble, France" (https://academic.oup.com/bioscience/article/67/3/201/2962463).