Antarctic bacterium Flavobacterium frigoris PS1 provides the source for this ice-binding protein. The dataset contains X-ray diffraction data for the FfIBP crystal, collected to a resolution of 2.9 Å, with unit-cell parameters a = b = 69.4, c = 178.2 Å. The data was reported by AMD_KOPRI in 2013.
Use Cases
- Compare protein crystal structures based on reported unit-cell parameters.
- Analyze antifreeze activity differences based on amino-acid sequence similarity to LeIBP.
- Model ice-binding mechanisms based on the crystal's space group P4122.
- Investigate thermal hysteresis activity based on the reported 2.5 K measurement.
Strengths
- Specific diffraction resolution of 2.9 Å is reported.
- Complete unit-cell parameters (a = b = 69.4, c = 178.2 Å) and space group (P4122) are provided.
- The protein source (Flavobacterium frigoris PS1 from Antarctica) and crystallization method are described.
Limitations
- Last updated 2013-09-24 00:00:00; freshness should be verified.
- Column-level documentation is absent; field semantics must be inferred after download.
- Row count is unknown, which may limit suitability assessment.
Provenance
- Source
- AMD_KOPRI
- Collection Method
- Data gathered from X-ray crystallographic experiments using the hanging-drop vapour-diffusion method.
- Geography
- Antarctic (source organism Flavobacterium frigoris PS1)