Leading Structural Biology & Drug Discovery Outsourcing Services

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

How did it all start?

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. These events of 1926 can be considered as the beginning of history of structural biology.

The First Diffraction Experiment, The First Protein Structures

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 Enters the Market

SARomics Biostructures entered the field of structural biology 80 years after the first crystals of urease were obtained. The company was founded by scientists with a mission to accelerate clients’ drug discovery projects by offering premium structural biology services. Starting with just one employee and a small crystallization room at the MAX II synchrotron, we developed a fully equipped platform with advanced technology to support structural biology and drug discovery. The platform includes protein cloning, expression, purification, biophysical characterization, crystallization, and structure determination using X-ray crystallography and NMR spectroscopy. Our fragment screening capabilities include proprietary fragment libraries and weak-affinity chromatography (WAC) technology, as well as NMR– and crystallographic fragment screening. Located at Medicon Village in Lund, near the 4th-generation MAX IV synchrotron, we provide priority access to the BioMAX and MicroMax beamlines, which are equipped for crystallographic fragment screening and serial crystallography experiments. Our FastLane library, which includes over 600 off-the-shelf drug target proteins for crystallization with our clients’ ligands and a turnaround time of just a few weeks, further contributes to accelerating clients’ drug discovery projects.

Over the past twenty years, we worked with the majority of the top ten pharmaceutical companies, many of the world’s most innovative biotech firms and academic groups across a broad range of drug-target classes. Many of the projects are documented in the extensive list of published papers, including 8 in Nature journals and more than 10 in other high-impact journals. Hundreds of disclosable crystal structures have been deposited in the Protein Data Bank (PDB), with many additional structures provided directly to clients.

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.