Directed by the U.S. Department of Energy's SLAC National Accelerator Laboratory with members from Arizona State University, an international team has demonstrated that a powerful X-ray laser can enable cracking the atomic code of biomolecules such as small protein present in egg whites.
The experiments carried out by the team were published in Science this week. It represented that ultrahigh-resolution views of nano-crystals of biomolecules was achieved using SLAC's Linac Coherent Light Source (LCLS). This will lead to creating critical new investigative approaches in biology.
An ASU Regents Professor of physics, John Spence said that a new 'snap-shot' X-ray laser method has been shown in this experiment where atomic-resolution images of proteins with femtosecond time resolution can be obtained without posing radiation harm to the sample.
According to Sébastien Boutet of LCLS, this first high-resolution demonstration represents 'diffraction-before-destruction' method on biological samples in which the sample is measured prior to being impacted by LCLS pulses.
Since several years, the shape of proteins and other biological molecules have been reconstructed via X-ray- illumination of crystallized samples to show its X-ray scattering property. Experimenting with the egg white protein called lysozyme involves the use of serial femtosecond crystallography in this first high-resolution experiment.
The technique has been demonstrated in the paper ‘High-resolution protein structure determination by serial femtosecond crystallography’. It operates at a higher resolution than earlier experimental work with X-ray lasers, through which scientists can use smaller crystals as well as view molecular dynamics at an improved time-scale.
With simple crystallizing property, lysozyme serves as the first research sample. These experiments help resolve the structure of lysozyme at high resolution. At this resolution, the researchers can differentiate the near identical amino acid sequences of a turkey from that of a hen lysozyme.