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.

For the first time in three years, LCLS has added a new instrument to its set of experimental stations. See photos of the brand new MFX hutch, LCLS’s seventh instrument.

The 2010 experiment marked a significant step forward in understanding extreme states of matter at the hearts of stars, planets and nuclear fusion reactions.

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.

A team led by SLAC scientists combined powerful magnetic pulses with some of the brightest X-rays on the planet to discover a surprising 3-D effect that appears linked to a mysterious phenomenon known as high-temperature superconductivity.

An all-day symposium recognized the professor emeritus for his many contributions to the scientific community, from pioneering synchrotron radiation research at SSRL to making science policies on Capitol Hill.

President Obama honored a SLAC and UCLA scientist for work that paved the way for the brightest sources of X-ray light on the planet.

A physicist at Argonne National Laboratory has been recognized for pioneering experiments at SLAC that helped establish a new way to study the structure of complex materials.

The former Stanford graduate student, who did extensive research at SLAC, is being honored as an exceptional role model for women in science.

The former SLAC and Stanford researcher will be recognized during a SLAC conference next month for her work in studying nanoscale magnetic and electronic processes.

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.