LCLS Coherent X-ray Imaging (CXI)
Scientists used SLAC's LCLS X-ray laser to make the first snapshots of a chemical interaction between two biomolecules. It changes the shape of millions of molecular switches almost instantaneously, like synchronized swimmers performing the same move.
The team determined the 3-D structure of a biomolecule by tagging it with selenium atoms and taking hundreds of thousands of images.
High-speed X-ray camera reveals ultrafast atomic motions at the root of organisms’ ability to turn light into biological function.
A new study with the LCLS X-ray laser could change the way researchers take atomic-level snapshots of important biological machineries, potentially affecting research in drug development, clean energy production and many more areas.
This surprising finding has potentially broad implications, from X-ray imaging of single particles to fusion research.
Researchers at SLAC have found a simple new way to study very delicate biological samples – like proteins at work in photosynthesis and components of protein-making machines called ribosomes – at the atomic scale using SLAC's X-ray laser.
The SLAC Photowalk took a group of 17 photographers, both amateur and professional, behind the scenes to photograph SLAC's world-class science facilities, including the Linac Coherent Light Source (LCLS) X-ray laser and the Stanford Synchrotron Radiation Lightsource (SSRL).
Using SLAC's X-ray laser, researchers have for the first time directly observed myoglobin move within quadrillionths of a second after a bond breaks and the protein releases a gas molecule.
A major international effort at SLAC is focused on improving our views of intact viruses, living bacteria and other tiny samples using the brightest X-ray light on Earth.
In a first-of-its-kind experiment, scientists got a textbook-worthy result that may change the way matter is probed at X-ray free-electron lasers.