Abstract
Crystallization conditions are reported for Streptomyces avidinii streptavidin with and without bound biotin. X-ray examination of the free and bound crystal forms shows the streptavidin-biotin complex crystals to be most suitable for high resolution structure analysis. A complete x-ray data set to 2.6 A resolution was collected for the streptavidin-biotin crystals using a two-dimensional area detector. Reduction and analysis of the x-ray diffraction pattern show that the complex crystallizes in the tetragonal space group I4(1)22 (a = b = 98.4 A, c = 125.8 A), with half of the streptavidin tetramer in the crystallographic asymmetric unit.
Highlights
X-ray examinat,ion of the free baonudnd crystal forms shows the streptavidin-biotin complex crystals to be most suitable for high resolution- structure analysis
Reduction and analysis of the x-ray diffraction pattern show that the complex crystalliFes in the tetrpgonal space group Z4,22 (a= b = 98.4 A, c = 125.8 A), with half of the streptavidin tetramer in the crystallographic asymmetric unit
Crystals of streptavidinandstreptavidin-biotin complex Laboratories, McLean, VA) in the usual manner [7]. Within were both grown by vapor diffusion using the hanging drop 2 weeks a t 4 “C, stacksof platelike crystals (typically 0.05 X technique[6].Biotin-freestreptavidincrystals were grown 0.2 X 0.2 mm) were observed over a wide range of solution buffer conditions including 0.1 M CAPS,pH 10.4, 0.1 M
Summary
Crystallization conditions are reported for Streptomyces avidinii streptavidin with and without bound biotin. X-ray examinat,ion of the free baonudnd crystal forms shows the streptavidin-biotin complex crystals to be most suitable for high resolution- structure analysis. A complete x-ray data set to2.6 A resolution was collected for the streptavidin-biotin crystals using a two-dimensional area detector.
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