Influence of X-ray Energies on Radiation Damage Using Lysozyme as a Tool
- Karolina Bobek
- Emily Formella
- Andrew Handzel
- Brinda Parikh
- Benjamin Roark
- Christa Thomas
- William Kane
- Karen Murphy
- Sahana Sukumar (Loyola University Chicago: College of Arts and Sciences)
- Narayanasami Sukumar (Argonne National Laboratory, NE-CAT)
Hen egg white lysozyme is one of the most studied proteins in biological crystallography. In this study, lysozyme is used as a model to investigate the effect of X-ray radiation damage on the structure of crystalline proteins. The advent of highly intense synchrotron beamlines has reintroduced the age-old problem of X-ray radiation damage in macromolecular crystallography, even for crystals held at cryogenic temperatures (100 K). Such damage to macromolecular crystalline samples during the experiment is an inherent problem when using ionizing radiation to obtain diffraction patterns and has presented a challenge to the crystallography field since the beginning.
One of the proposed analyses is to study the effect of radiation damage on disulfide bonds with respect to X-ray energies. Disulfide bonds contribute to stabilization of tertiary structure of lysozyme. Lysozyme has four disulfide bonds which consists of the two intra-α-domain disulfides, the intra-β-domain, and the inter-αβ-domains.