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Cited by 588

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

Open access
Hendrickson, W A, Pähler, A, Smith, J L, Satow, Y, Merritt, E A, Phizackerley, R P·1989·Proceedings of the National Academy of Sciences

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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Metadata

Authors
Hendrickson, W. A., Pähler, A., Smith, J. L., Satow, Y., Merritt, E. A., & Phizackerley, R. P.
Venue
Proceedings of the National Academy of Sciences
Published
1989-04
Volume
86
Issue
7
Pages
2190-2194
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2027836552
Cited by
588
References
1
FWCI
18.58
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation. https://app.cochat.ai/papers/10.1073/pnas.86.7.2190
The paper
Hendrickson, W. A., Pähler, A., Smith, J. L., Satow, Y., Merritt, E. A., & Phizackerley, R. P. (1989). Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.86.7.2190

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