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PMID: 2928324 Published · ppublish English Journal Article 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.

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

Hendrickson WA, Pähler A, Smith JL, Satow Y, Merritt EA, Phizackerley RP

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.

MeSH Terms
Bacterial Proteins Biotin Macromolecular Substances Models, Molecular Particle Accelerators Protein Conformation Scattering, Radiation Spectrum Analysis Streptavidin
Chemicals
Bacterial Proteins Macromolecular Substances Biotin Streptavidin
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Hendrickson W A
Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY.
Pähler A
Smith J L
Satow Y
Merritt E A
Phizackerley R P
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1989-04-00
Pages
2190-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC286877
Subset
IM
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