Researchers at the SLAC National Accelerator Laboratory recently used the Linac Coherent Light Source (LCLS) laser to visualize crystallized biomolecules such as lysozymes, which are small proteins found in egg whites.

In the past, scientists have used X-rays to analyze the structure of biological molecules by observing how a molecule scatters X-ray beams. With the help of the LCLS, SLAC led an international team of researchers to use an imaging technique called serial femtosecond crystallography, which gathers an image by the emission of ultrashort, ultrabright X-ray laser pulses lasting one femtosecond (10^-15 seconds), to obtain a high-resolution image of the molecule in question.

The advantage of this high-resolution technique is that scientists can now use smaller crystals than in X-ray refraction analysis and can gain different insight into molecular dynamics, according to a SLAC press release.

Researchers said they used lysozyme as their first research sample because it is easily crystallized. However, the team plans to use the same technique to image more-complex proteins in the future.

This was the first study to use the Coherent X-Ray Imaging (CXI) instrument at SLAC. The CXI device is a type of molecular camera that can image biological samples to a point of damage beyond which other molecular cameras cannot produce images.

The results of the experiment were published in Science.

The international team included researchers from Max Planck Institutes, DESY, Arizona State University, Cornell University, SUNY Oswego, The Johns Hopkins University Applied Physics Laboratory, the Nikhef National Institute for Subatomic Physics, the European Synchrotron Radiation Facility, the University of Gothenburg, the University of Hamburg, the University of Lübeck and Uppsala University.

— Alice Phillips