Drosophila Calmodulin Crystal Structure Refined at 2.2-Angstrom Resolution

2.2-Angstrom resolution crystal structure of recombinant calmodulin from Drosophila melanogaster, refined with a crystallographic R value of 0.197. The model includes 1,164 protein atoms, 4 calcium ions, and 78 water molecules, revealing structural differences from mammalian calmodulin. The data was produced by Denise Taylor of the Howard Hughes Medical Institute.

Use Cases

• Comparative protein structure analysis based on root mean square deviation values for equivalent atoms.
• Studying calcium-binding site geometry based on the four 'EF hand' sites described.
• Analyzing the impact of conservative amino acid changes on protein conformation.
• Modeling the structure of the 'dumb-bell' shaped molecule with its seven alpha-helices and central helix bend.

Strengths

• High-resolution structural data refined at 2.2-Angstroms.
• Model includes precise atomic coordinates with root mean square deviations of 0.018 Å for bond lengths and 0.043 Å for angle distances.
• Includes 4 calcium ions and 78 water molecules in the refined model.

Limitations

• Row count and specific column-level documentation are unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.
• Data may reflect the specific experimental and crystallographic bias inherent to the source platform.

Provenance

Source

Howard Hughes Medical Institute

Collection Method

X-ray crystallography of bacterially expressed protein, with structure refinement starting from a mammalian calmodulin model.