Thermitase Crystallographic Studies at 0, 5, and 100 mM Calcium Concentrations

Three crystal structures of thermitase complexed with eglin-c have been determined, including one refined at 2.0-Å resolution to an R-factor of 16.8%. The dataset compares structural changes at three calcium binding sites across different calcium concentrations. The data was produced by Piet Gros of the University of Groningen.

Use Cases

• Analyzing calcium ion coordination geometry based on the described pentagonal bipyramid and square antiprism arrangements.
• Comparing protein conformational changes based on the 0.8-Å difference in C alpha positions for ligand Asp-60.
• Studying cation binding site occupancy and competition between monovalent and divalent ions as described for the 'weak' site.
• Modeling long-range structural shifts in enzymes by comparing thermitase to subtilisin BPN' and proteinase K as referenced.

Strengths

• Includes a structure refined at 2.0-Å resolution with an R-factor of 16.8%.
• Compares three distinct calcium concentration conditions (0, 5, and 100 mM).
• Describes specific geometric arrangements and ligand coordination for three binding sites.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

Piet Gros, University of Groningen

Collection Method

X-ray crystallography studies, likely from published research.