X-ray diffraction data from crystallographic experiments on the ice-binding protein LeIBP produced by Arctic yeast Leucosporidium sp. The protein has a molecular mass of approximately 25 kDa and exhibits low sequence similarity to known antifreeze proteins. The dataset was produced by AMD_KOPRI and last updated in June 2012.
Use Cases
- Analyze protein crystal diffraction patterns based on X-ray crystallographic experiments
- Compare structural features of LeIBP with other antifreeze proteins based on low amino acid sequence similarity
- Investigate antifreeze mechanisms based on the protein's ability to lower freezing points
Strengths
- Data is derived from a recombinant protein expression system allowing high-level production and efficient purification
- The protein's molecular mass of approximately 25 kDa is explicitly stated
Limitations
- Description metadata is limited; actual data quality requires manual inspection after download
- Last updated 2012-06-26 00:00:00; freshness should be verified
- Column-level documentation is absent; field semantics must be inferred after download
Provenance
- Source
- AMD_KOPRI
- Collection Method
- Preliminary X-ray crystallographic experiments