#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