title: Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation.
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.
authors.affiliation: Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY.
authors.forename: W A
authors.initials: WA
authors.lastname: Hendrickson
authors.forename: A
authors.initials: A
authors.lastname: Pähler
authors.forename: J L
authors.initials: JL
authors.lastname: Smith
authors.forename: Y
authors.initials: Y
authors.lastname: Satow
authors.forename: E A
authors.initials: EA
authors.lastname: Merritt
authors.forename: R P
authors.initials: RP
authors.lastname: Phizackerley
mesh_terms: D001426:Bacterial Proteins; D001710:Biotin; D046911:Macromolecular Substances; D008958:Models, Molecular; D010315:Particle Accelerators; D011487:Protein Conformation; D012542:Scattering, Radiation; D013057:Spectrum Analysis; D019809:Streptavidin
chemical_list: D001426:Bacterial Proteins; D046911:Macromolecular Substances; D001710:Biotin; D019809:Streptavidin