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

摘要: Abstract A three-dimensional crystal structure of the biotin-binding core streptavidin has been determined at 3.1-A resolution. The was analyzed from diffraction data measured three wavelengths a single selenobiotinyl complex with streptavidin. Streptavidin is tetramer subunits arrayed in D2 symmetry. Each protomer an 8-stranded beta-barrel simple up-down topology. Biotin molecules are bound one end each barrel. This study demonstrates effectiveness multiwavelength anomalous (MAD) procedures for macromolecular crystallography and provides basis detailed biotin-avidin interactions.