構造決定の手法: 分子置換 / 解像度: 2→18.98 Å / Cor.coef. Fo:Fc: 0.918 / Cor.coef. Fo:Fc free: 0.893 / SU R Cruickshank DPI: 0.182 / 交差検証法: FREE R-VALUE / σ(F): 0 / SU R Blow DPI: 0.187 / SU Rfree Blow DPI: 0.168 / SU Rfree Cruickshank DPI: 0.166 詳細: Intensities of only approx. 64 degrees of the data collection sweep were merged and used for model refinement. Subsequent diffraction images show ice rings, possibly due to malfunctioning ...詳細: Intensities of only approx. 64 degrees of the data collection sweep were merged and used for model refinement. Subsequent diffraction images show ice rings, possibly due to malfunctioning crystal cooling. The protein was crystallized in the presence of a putative inhibitor, but electron density maps did not fully resolve the expected inhibitor.