A sub-ångström-resolution atomic structure of a protofibril formed by a wild-type segment (QYNNQNNFV) from the β2-α2 loop of the bank vole prion protein. The structure was determined using the cryo-EM method MicroED by C. Glynn at the University of California, Los Angeles. It reveals a stabilizing network of hydrogen bonds and motifs named 'polar clasps'.
Use Cases
- Modeling prion protein misfolding based on the revealed protofibril structure.
- Studying hydrogen bond networks in protein aggregates based on the described 'polar clasps'.
- Benchmarking cryo-EM structure determination methods using the sub-ångström-resolution data.
Strengths
- Structure determined at sub-ångström resolution, indicating high precision.
- Data originates from a study published via the Open Access (green) license.
- Focuses on a specific wild-type protein segment (QYNNQNNFV) from bank vole prion protein.
Limitations
- Row count is unknown, which may limit suitability assessment.
- Column-level documentation is absent; field semantics must be inferred after download.
- Last update date is unknown; freshness unverified.
Provenance
- Source
- University of California, Los Angeles
- Collection Method
- Cryo-EM method MicroED