#SyncroLightAt75 – Structure of the Ribosome

Along with Ada Yonath and Thomas Steitz,Venkatraman Ramakrishnan from the MRC Laboratory of Molecular Biology in Cambridge, UK was awarded the 2009 Nobel Prize in Chemistry for determining the structure of the ribosome, one of the largest and most important molecules in the cell. X-ray crystallography experiments that enabled elucidation of the ribosome structure used synchrotron light from a number of light sources worldwide, each with unique capabilities, including the Swiss Light Source SLS.

Read more on the PSI website

Image: Interior view of the experimental hall at the Swiss Light Source SLS

Credit: Photo: H.R. Bramaz/PSI

#SynchroLightAt75 – From the Ribosome to CRISPR

Structural Biology at the ALS: From the Ribosome to CRISPR

Since the first protein crystallography beamline came online here in 1997, thousands of protein structures have been solved at the Advanced Light Source (ALS). One of the earliest high-profile structures was that of the full ribosome complex, where all the proteins necessary for life are produced based on RNA blueprints. The results reinforced the impression that the ribosome is a dynamic molecular machine with moving parts and a very complicated mechanism of action. More recently, the ALS has contributed to a greater understanding of programmable CRISPR proteins such as Cas9. In contrast to earlier genome-editing tools, Cas9 transforms the complicated and expensive process of gene editing into something simpler and more routine, like applying a genetic plug-in. In 2020, Jennifer Doudna and Emmanuelle Charpentier were awarded the Nobel Prize in Chemistry for “the development of a method for genome editing.”

Read more in the links below:


J.H. Cate et al., Science 285, 2095 (1999)

M. Jinek et al., Science 343, 1247997 (2014)

Press release: The Nobel Prize in Chemistry 2020

ALS highlights:

Solving the Ribosome Puzzle
Intriguing DNA Editor (CAS9) Has a Structural Trigger

Jennifer Doudna and the Nobel Prize: The Advanced Light Source Perspective

#SynchroLightAt75 – APS lights the way to 2012 Chemistry Nobel

Thanks in part to research performed at the U.S. Department of Energy’s (DOE) Argonne National Laboratory, the 2012 Nobel Prize in Chemistry was awarded today to Americans Brian Kobilka and Robert Lefkowitz for their work on G-protein-coupled receptors.

G-protein-coupled receptors, or GPCRs, are a large family of proteins embedded in a cell’s membrane that sense molecules outside the cell and activate a cascade of different cellular processes in response. They constitute key components of how cells interact with their environments and are the target of nearly half of today’s pharmaceuticals.

These medicines work by connecting with many of the 800 or so human GPCRs. But to do this well, a drug needs to connect to the protein like a key opens a lock. Improving drugs requires knowing exactly how these proteins work and are structured, which is difficult because the long, slender protein chains are folded in an intricate pattern that threads in and out of the cell’s membrane.

In a study performed at Argonne in 2007, Kobilka, a professor at Stanford University, used intense X-rays produced by the laboratory’s Advanced Photon Source (APS) to make the first discovery of the structure of a human GPCR. This receptor, called the human β2 adrenoreceptor (β2AR), is responsible for a number of different biological responses, including facilitating breathing and dilating the arteries.

Read more on the Argonne National Laboratory website

Image: This is an image of a G-protein-coupled receptor signaling complex whose structure was identified in 2011. The receptor is in magenta while the different G protein subunits are colored green, red and blue. Stanford biochemist Brian Kobilka shared the 2012 Nobel Prize in Chemistry for his work in determining the structure of this activated GPCR using X-rays provided by Argonne’s Advanced Photon Source.

#SynchroLightAt75 – Rod MacKinnon’s Nobel Prize in chemistry

Rod MacKinnon – Nobel Prize in chemistry 2003 for work on the structure of ion channels  

The structural work of MacKinnon was carried out primarily at the Cornell High Energy Synchrotron Source (CHESS) and the National Synchrotron Light Source (NSLS) at Brookhaven. At the time, CHESS was a first-generation SR source.  The award for MacKinnon’s work was the second recognition of SR work by the Nobel Committee. MacKinnon acknowledges the crucial role that the two synchrotron facilities, Cornell Synchrotron (CHESS/MacCHESS) and NSLS, have played in his research on the protein crystallography of membrane channels.

He said, `Without exaggeration that most of what is known about the chemistry and structure of ion channels has come from experiments carried out at these SR centres’.

Rod MacKinnon

Read more on the Nobel Prize website

Image: View showing the location of CHESS, which is underground at Cornell

Credit: Jon Reis

#SynchroLightAt75 – Photon Factory at the dawn of structural biology using SR

The Photon Factory opened its first dedicated protein crystallography beamline with a Weissenberg camera in the mid-1980s. Prof. Ada Yonath, who was awarded the Nobel Prize in Chemistry in 2009 for her work on the structure-function analysis of ribosomes, was working at the Photon Factory at this time. The cryo-crystallography developed at the time led to the successful structural analysis.

Read more about the 2009 Nobel Prize in Chemistry and KEK’s Photon Factory here: KEK feature article

Image: Cryo-cooling system developed by Prof. Ada Yonath installed at the Photon Factory

Credit: Photo courtesy of Prof. Noriyoshi Sakabe