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Crystal Structure of Core Streptavidin Determined from Multiwavelength Anomalous Diffraction of Synchrotron Radiation
Wayne A. Hendrickson, Arno Pahler, Janet L. Smith, Yoshinori Satow, Ethan A. Merritt and R. Paul Phizackerley
Proceedings of the National Academy of Sciences of the United States of America
Vol. 86, No. 7 (Apr. 1, 1989), pp. 2190-2194
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/33443
Page Count: 5
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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 D2 symmetry. Each protomer is an 8-stranded β -barrel with simple up-down topology. Biotin molecules are bound at one end of each barrel. This study demonstrates the effectiveness of multiwavelength anomalous diffraction (MAD) procedures for macromolecular crystallography and provides a basis for detailed study of biotinavidin interactions.
Proceedings of the National Academy of Sciences of the United States of America © 1989 National Academy of Sciences