Guarav "Gino" Giri, who this summer completed his doctoral work in chemical engineering at Stanford, has been selected to receive this year's Melvin P. Klein Scientific Development Award for his pioneering work aimed at understanding and improving organic semiconductor performance and developing new production methods.
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.