In a new state-of-the-art lab at SLAC National Accelerator Laboratory, components of ribosomes – tiny biological machines that make new proteins and play a vital role in gene expression and antibiotic treatments – form crystals in a liquid solution.
Signs at the lab's entryway warn of the potential for contamination – these delicate samples can be damaged by human touch, a sneeze or a dust particle.
In an advance that will help scientists design and engineer proteins, a team including researchers from SLAC and Stanford has found a way to identify how protein molecules flex into specific atomic arrangements required to catalyze chemical reactions essential for life.
A new tool at SLAC's Linac Coherent Light Source splits individual X-ray laser pulses into two pulses that can hit a target one right after another with precisely controlled timing, allowing scientists to trigger and measure specific ultrafast changes in atoms and molecules.
It all comes down to one tiny spot on a diamond-cut, highly pure copper plate. That's where every X-ray laser pulse at SLAC's Linac Coherent Light Source gets its start. That tiny spot must be close to perfect or it can impair and even halt LCLS operations.
SLAC in May 2013 opened a new test facility at the Accelerator Structure Test Area (ASTA) to study the complex physics and chemistry that cause that shiny copper slab, called a cathode, to degrade over time, and to identify ways to maintain and improve its performance.
Pushing gold exploration to the nanoscale, scientists used SLAC's Linac Coherent Light Source X-ray laser to produce a series of 3-D images that detail a ringing effect in tiny gold crystals. The technique provides a unique window for studying why smaller is better for some specialized materials, including those used in chemical reactions and electronic components, for example.