CRYSTAL-STRUCTURE OF CORE STREPTAVIDIN DETERMINED FROM MULTIWAVELENGTH ANOMALOUS DIFFRACTION OF SYNCHROTRON RADIATION
CRYSTAL-STRUCTURE OF CORE STREPTAVIDIN DETERMINED FROM MULTIWAVELENGTH ANOMALOUS DIFFRACTION OF SYNCHROTRON RADIATION
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DOI:
10.1073/pnas.86.7.2190
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发表时间:
1989-04-01
影响因子:
11.1
通讯作者:
PHIZACKERLEY, RP
中科院分区:
文献类型:
--
作者:
HENDRICKSON, WA;PAHLER, A;PHIZACKERLEY, RP
A three-dimensional crystal structure of the biotin-binding core of streptavidin has been determined at 3.1 .ANG. 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 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.