Se-SAD serial femtosecond crystallography datasets from selenobiotinyl-streptavidin.

ABSTRACT: We provide a detailed description of selenobiotinyl-streptavidin (Se-B SA) co-crystal datasets recorded using the Coherent X-ray Imaging (CXI) instrument at the Linac Coherent Light Source (LCLS) for selenium single-wavelength anomalous diffraction (Se-SAD) structure determination. Se-B SA was chosen as the model system for its high affinity between biotin and streptavidin where the sulfur atom in the biotin molecule (C₁₀H₁₆N₂O₃S) is substituted with selenium. The dataset was collected at three different transmissions (100, 50, and 10%) using a serial sample chamber setup which allows for two sample chambers, a front chamber and a back chamber, to operate simultaneously. Diffraction patterns from Se-B SA were recorded to a resolution of 1.9 Å. Th

SUBMITTER: Yoon CH 

PROVIDER: S-EPMC5404608 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature