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

W A Hendrickson; A Pähler; J L Smith; Y Satow; E A Merritt; R P Phizackerley

doi:10.1073/pnas.86.7.2190

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

Proc Natl Acad Sci U S A. 1989 Apr;86(7):2190-4. doi: 10.1073/pnas.86.7.2190.

Authors

W A Hendrickson¹, A Pähler, J L Smith, Y Satow, E A Merritt, R P Phizackerley

Affiliation

¹ Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY.

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Bacterial Proteins*
Biotin
Macromolecular Substances
Models, Molecular
Particle Accelerators
Protein Conformation
Scattering, Radiation
Spectrum Analysis
Streptavidin

Substances

Bacterial Proteins
Macromolecular Substances
Biotin
Streptavidin