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Structural effects of radiation damage and its potential for phasing
Sankaran Banumathi1, Petrus H Zwart, Udupi A Ramagopal
1Synchotron Radiation Research Section, MCL, National Cancer Institute, Brookhaven National Laboratory, Upton, NY 11973, USA.
Summary
Radiation damage to thaumatin causes structural changes, including disulfide bond breakage. These changes, particularly to sulfur atoms, aided in phasing protein structures, even at low resolution.
Area of Science:
- Structural biology
- Protein crystallography
- Radiation damage studies
Background:
- Understanding radiation damage is crucial for macromolecular crystallography.
- Thaumatin serves as a model protein for studying radiation effects.
Purpose of the Study:
- To analyze radiation-damage-induced structural and intensity changes in thaumatin.
- To investigate the utility of radiation-induced sulfur atom changes for phasing.
Main Methods:
- Detailed analysis of X-ray diffraction data from irradiated thaumatin.
- Application of the radiation-induced phasing (RIP) procedure.
- Utilizing ACORN software for structure determination.
Main Results:
- Reflection intensity changes exhibited a parabolic pattern upon irradiation.
- Key structural alterations included disulfide bond breakage and residue decarboxylation.
- Successful high-quality phase estimates were obtained using sulfur atom changes via RIP.
- ACORN results indicated the importance of partial structure contributions in phasing.
Conclusions:
- Radiation damage significantly alters protein structure and diffraction intensities.
- Sulfur atom changes induced by radiation are valuable for phasing in crystallography.
- Partial structure information is beneficial for phasing, even below atomic resolution.
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