Crystal Structure of Core Streptavidin Determined from Multiwavelength Anomalous Diffraction of Synchrotron Radiation

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 te...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1989-04, Vol.86 (7), p.2190-2194
Main Authors: Hendrickson, Wayne A., Pahler, Arno, Smith, Janet L., Satow, Yoshinori, Merritt, Ethan A., Phizackerley, R. Paul
Format: Article
Language:English
Subjects:
Absorption spectra
Bacterial Proteins
Biological and medical sciences
Biotin
Crystal structure
Crystalline structure
Crystals
Electrical phases
Fundamental and applied biological sciences. Psychology
Macromolecular Substances
Models, Molecular
Molecular biophysics
Molecules
Particle Accelerators
Photons
Protein Conformation
Scattering, Radiation
Selenium
Spectrum Analysis
Streptavidin
Structure in molecular biology
Synchrotron radiation
Wave diffraction
Wavelengths
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.86.7.2190