Crystallographic data for Streptomyces avidinii streptavidin

Area of Science:

• Structural Biology
• Biochemistry
• Crystallography

Background:

• Streptavidin, a protein from Streptomyces avidinii, is known for its high affinity for biotin.
• Understanding the structure of the streptavidin-biotin complex is vital for various applications, including diagnostics and therapeutics.

Purpose of the Study:

• To determine the crystallization conditions for Streptomyces avidinii streptavidin.
• To analyze the crystal structure of the streptavidin-biotin complex at high resolution.

Main Methods:

• X-ray diffraction analysis of crystallized Streptomyces avidinii streptavidin.
• Data collection using a two-dimensional area detector to 2.6 A resolution.
• Analysis of X-ray diffraction patterns to determine space group and unit cell dimensions.

Main Results:

• Crystallization conditions were established for both free and biotin-bound Streptomyces avidinii streptavidin.
• The streptavidin-biotin complex crystallized in the tetragonal space group I4(1)22.
• A complete X-ray data set to 2.6 A resolution was obtained, suitable for detailed structural analysis.

Conclusions:

• The streptavidin-biotin complex crystals are optimal for high-resolution structure determination.
• The crystallographic data provide a foundation for understanding the precise molecular interactions between streptavidin and biotin.