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Celebrating 100 Years of Structural Biology and 20 Years of SARomics Biostructures!

On June 2, 1926, a manuscript by James B. Sumner (Department of Physiology and Biochemistry, Cornell University Medical College, Ithaca) titled “THE ISOLATION AND CRYSTALLIZATION OF THE ENZYME UREASE” was received for publication in J. Biol. Chem. In the introduction, the author writes, “I discovered on the 29th of April a means of obtaining from the jack bean a new protein which crystallizes beautifully and whose solutions possess to an extraordinary degree the ability to decompose urea into ammonium carbonate”. This was the first time protein crystals were described as “beautiful”, an expression so familiar to all protein crystallographers! At a time when proteins were thought to be a type of colloids, Sumner demonstrated for the first time that they possessed a defined and stable atomic structure and could crystallize. Additionally, he showed that enzymes were actually proteins.
Another remarkable publication of 1926 was by T. Svedberg and R. Fåhraeus, published in JACS with the title “A new method for the determination of the molecular weight of the proteins”, in which, for the first time, the molecular weight of hemoglobin was determined by analytical centrifugation to be 66 kDa.

Eight years later, in 1934, the first report of X-ray diffraction by a protein crystal was published. This was a Nature paper by J. D. Bernal and D. Crowfoot, titled “X-ray photographs of crystalline pepsin”. The authors mention that the protein was crystallized by Dr. Philpot in the Laboratory of Prof. The Svedberg in Uppsala and brought to Cambridge by Dr. G. Millikan. Still, the world had to wait 24 more years until the first protein structure was finally determined. After solving the phase problem, J. C. Kendrew et al., in 1958, reported the structure of myoglobin, and in 1960, M. F. Perutz et al. published the structure of hemoglobin. In 1962, they were awarded the Nobel Prize in Chemistry. This marked the beginning of a long chain of Nobel Prizes awarded for work in structural biology, the most recent in 2024 for the development of computational methods for protein structure prediction. The Nobel Committee stated, “David Baker has succeeded with the almost impossible feat of building entirely new kinds of proteins. Demis Hassabis and John Jumper have developed an AI model to solve a 50-year-old problem: predicting proteins’ complex structures”. Since the first protein crystals were obtained, structural biology has developed into an interdisciplinary field within modern biological sciences that employs a range of complementary biophysical techniques to examine biological structures and functional processes at the atomic level.

SARomics Biostructures entered the field of structural biology 80 years after the first publication describing urease crystallization. Starting with just one employee and a small crystallization room at the MAX II synchrotron, we developed a fully equipped technical platform for structural biology research, including protein cloning, expression, purification, characterization, and crystallization. Today, SARomics Biostructures offers a broad range of structural biology services, including protein structure determination using X-ray crystallography and NMR spectroscopy, fragment library screening with weak-affinity chromatography (WAC™), NMR spectroscopy, and crystallographic fragment screening. Over the past two decades, the team has worked with many drug-target classes, providing high-quality structural biology services to the biotech and pharmaceutical industries.

Below is a more detailed description of our services. Additional information about our experimental platform can be found in our technology platform overview and on our blog.