BulkArg: computational pipeline for improving protein crystallization propensity
This technology is a computational pipeline which predicts arginine substitutions in a protein at select lysine sites to improve protein crystallization efficiency.
Unmet Need: Method for improving recalcitrant protein crystallization efficiency
Protein crystallization is a critical step for elucidating protein structures and drug-target interactions by X-ray crystallography. However, only 9.8% of expressed proteins generate crystals of sufficient size and quality for X-ray screening. There are currently no reproducible methods for crystallizing recalcitrant proteins.
The Technology: Computational pipeline for improving crystallization of recalcitrant proteins
This technology describes a computational pipeline which identifies lysine sites in recalcitrant proteins that can be substituted for arginine to improve crystallization. This technology identifies arginine substitutions at favorable sites which conserve protein structures. This method allows for a two week turn-around time from protein expression to a crystal structure, significantly reducing the amount of time it would typically take for a recalcitrant protein structure to be resolved.
This technology has been validated on two publicly available protein structures and one protein without a publicly available protein structure.
Applications:
- Protein engineering for altered protein structure/activity
- Resolving protein structures
- Resolving drug-target interactions
- Crystallization of antibody-antigen complexes
Advantages:
- Expedites protein crystallization
- Improves protein crystallization propensity
- Identifies specific amino acid substitutions
- Conserves protein structures
Lead Inventor:
Patent Information:
Patent Pending
Related Publications:
Tech Ventures Reference:
IR CU23101
- Licensing Contact: Beth Kauderer