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Crystal structure of core streptavidin determined from multi-wavelength anomalous diffraction of synchrotron radiation

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
A three-dimensional crystal structure of the biotin-binding core of streptavidin has been determined at 3.1-{angstrom} resolution. The structure was analyzed from diffraction data measured at three wavelengths from a single crystal of the selenobiotinyl complex with streptavidin. Streptavidin is a tetramer with subunits arrayed in D{sub 2} symmetry. Each protomer is an 8-stranded {beta}-barrel with simple up-down topology. Biotin molecules are bound at one end of each barrel. This study demonstrates the effectiveness of multi-wavelength anomalous diffraction (MAD) procedures for macromolecular crystallography and provides a basis for detailed study of biotin-avidin interactions.
OSTI ID:
5350773
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 86:7; ISSN PNASA; ISSN 0027-8424
Country of Publication:
United States
Language:
English