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The three-dimensional structure of the peptide was determined by X-ray diffraction method and refined to an R-factor of 0.065.
Two-dimensional (2D) branches were roughly segmented from the image by the "stripe programming" method, and refined by the ribbon snake model.
The molecule structure was further confirmed by PXRD based crystal structure, which was solved following direct space method and refined by the Rietveld method.
The EBOV NPcore was successfully crystallized, and the crystal structure was subsequently determined using the single-wavelength anomalous dispersion (SAD) method and refined to a high resolution of 1.8 Å with a final R work of 19.2% (R free = 22.3%) (Table 1).
The structure of CrSPI-1-D1 wasolveded by molecular replacement method and refined to a final R-factor of 0.21 (Rfree = 0.25) at 2.0 Å resolution.
The structures were solved by MAD phasing method and refined with CNS program package (31).
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Using Olex241, the structure was solved with the ShelXT42 structure solution program using Direct Methods and refined with the ShelXL42 refinement package using Least Squares minimization.
The structure was solved by direct methods and refined by full-matrix least-squares on F2 using the Bruker SHELXTL package (Supplementary Notes 2 and 3).
The diffraction data were collected on the KEK Photon Factory, the complex structures were determined by Molecular replacement methods and refined by PHINEX software package.
The crystal structures of these compounds were solved by direct methods and refined by full-matrix least squares.
The structure was determined by direct methods and refined by least-squares procedure to an R factor of 0.082.
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