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. 1989 Apr;86(7):2190–2194. doi: 10.1073/pnas.86.7.2190

Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation.

W A Hendrickson 1, A Pähler 1, J L Smith 1, Y Satow 1, E A Merritt 1, R P Phizackerley 1
PMCID: PMC286877  PMID: 2928324

Abstract

A three-dimensional crystal structure of the biotin-binding core of streptavidin has been determined at 3.1-A 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 beta-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 biotin-avidin interactions.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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