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"With these unique X-rays, we can perform truly damage-free measurements of structural and electronic properties. This paves the way for advanced studies like attosecond crystallography, allowing us to observe electronic dynamics in real space."

Researchers then accessed physical models of the two proteins that were produced using complex microscopy and x-ray crystallography techniques.

Using a technique called protein crystallography, they were able to view the atoms of the protein interacting with serine.

The researchers combined X-ray crystallography and cryo-EM to study the 3D structure of egg coat proteins.

For the study, recently published online in the journal Nature Chemical Biology, the team used X-ray crystallography to study NinaB, a protein found in insects that functions similarly to the RPE65 protein found in humans.