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.
“Ribosomes are more fragile than typical protein crystals,” said Hasan Demirci, a visiting investigator from Brown University who set up the ultraclean laboratory at SLAC this year to grow the ribosome crystals. “They are like marshmallows.” Since they have far fewer sides, or facets, than most crystallized proteins, their structure, or lattice, is easily punctured and wrecked. “You have to be so careful when you harvest them or they will lose their quality,” he said.
While the function of ribosomes is well understood, the details of how they work are not, and Demirci hopes his work at SLAC will supply new insights into the timing and chronology of ribosomes at work.
His work got an important boost in March, when he was selected to participate in a test program to study his crystals at SLAC’s Linac Coherent Light Source X-ray laser for the first time.
The ultrashort, ultrabright X-ray pulses at LCLS can be used to explore the structure and other properties of crystallized samples in the instant before they are destroyed. LCLS can also be used to study very small crystals, at room temperature and in a liquid solution.
Read more at: Phys.org