## 3 Results
### Data Dissection  
Large crystals provide diffraction data without intensity problems up to a certain rotation angle; however, theoretically, radiation damage always occurs at the center of the crystal where the X-ray was aligned. Accordingly, it is important to collect data that can minimize radiation damage to generate a better model structure. Thaumatin\({}^{100 ms}\) data were split into 90\({}^{\circ}\) increments and reprocessed, and structure refinement was performed (Table 3). Figure 5: 2 mFo-DFc (blue mesh, 1\(\sigma\)) and mFo-DFc (green mesh, 3\(\sigma\); red mesh, \(-3\sigma\)) electron density map of disulfide bonds in (**A**) Thaumatin\({}^{1s}\) and (**B**) Thaumatin\({}^{100 ms}\). (Upper) 2 mFo-DFc and mFo-DFc; (lower) mFo-DFc. \begin{table}
\begin{tabular}{c c c c c} \hline \hline
**Data Reprocessing** & **Data I** & **Data II** & **Data III** & **Data III** \\ \hline Processed image range (\({}^{\circ}\)) & 1–90 & 91–180 & 181–270 & 271–360 \\ Space group & P4\({}_{1}\)2\({}_{1}\)2 & P4\({}_{1}\)2\({}_{1}\)2 & P4\({}_{1}\)2\({}_{1}\)2 & P4\({}_{1}\)2\({}_{1}\)2 \\ \(a\), \(b\), \(c\) (Å) & 57.95, 57.95, 150.37 & 57.79, 57.79, 150.32 & 57.97, 57.97, 150.60 & 57.85, 57.85, 150.554 \\ \(\alpha\), \(\beta\), \(\gamma\) (\({}^{\circ}\)) & 90, 90, 90 & 90, 90, 90 & 90, 90, 90 & 90, 90, 90 \\ Resolution range (Å) & 40.98–1.15 & 45.82–1.18 & 45.94–1.17 & 45.87–1.26 \\  & (1.19–1.15) & (1.22–1.18) & (1.21–1.17) & (1.30–1.26) \\ Total No. of reflections & 561,360 (54,650) & 516,593 (49,690) & 533,885 (51,881) & 430,190 (41,752) \\ No. of unique reflections & 91,682 (9039) & 84,214 (8292) & 87,349 (8625) & 69,635 (6843) \\ Completeness (\%) & 99.79 (99.78) & 99.49 (99.89) & 99.78 (99.75) & 99.47 (99.87) \\ Multiplicity & 6.1 (6.0) & 6.1 (6.0) & 6.1 (6.0) & 6.2 (6.1) \\ Mean I/sigma (I) & 7.30 (1.20) & 7.55 (1.29) & 7.27 (1.00) & 7.31 (1.25) \\ CC1/2 & 0.998 (0.624) & 0.997 (0.601) & 0.997 (0.499) & 0.996 (0.561) \\ CC\({}^{*}\) & 0.999 (0.877) & 0.999 (0.867) & 0.999 (0.816) & 0.999 (0.848) \\ Wilson B factor & 10.60 & 10.42 & 11.92 & 12.00 \\ \hline \hline \end{tabular}
\end{table} 
Table 3: Data and refinement statistics of reprocessed Thaumatin\({}^{100 ms}\). The images of Thaumatin\({}^{100\rm ms}\) at 1-90\({}^{\circ}\) (Data I), 91-180\({}^{\circ}\) (Data II), 181-270\({}^{\circ}\) (Data III), and 271-360\({}^{\circ}\) (Data IV) were processed up to 1.15, 1.18, 1.17, and 1.26 A, respectively (Table 3). The results indicated that Data IV had a relatively reduced diffraction limit compared with the other data. The Wilson B factors of Data I, Data II, Data III, and Data VI were 10.60, 10.42, 11.92, and 12.00 A\({}^{2}\), respectively, indicating that Data I and II were relatively lower than Data III and Data IV, which were collected later. There were no significant differences in terms of completeness or CC1/2. Meanwhile, among the four datasets, radiation damage was theoretically minimized in Data I, and this was compared with the Thaumatin\({}^{100\rm ms}\) (1-360\({}^{\circ}\)) data collection statistics. Thaumatin\({}^{100\rm ms}\) (1-360\({}^{\circ}\)) was higher than Data I in terms of resolution and I/sigma; however, the Wilson B-factor indicated that Data I represented an improvement over the total image. Next, refinement was performed using the Thaumatin\({}^{100\rm ms}\) model for each dataset at 1.3 A resolution to allow for quantitative comparisons. The R\({}_{\rm work}\)/R\({}_{\rm free}\) of Data I, Data II, Data III, and Data IV were 15.67/17.33, 15.70/16.56, 16.03/17.12, and 16.23/16.83, respectively. The average protein B-factors of Data I, Data II, Data III, and Data IV were 11.85, 12.89, 13.27, and 13.92, respectively. In terms of B-factor, Data I at the beginning was excellent; however, it was difficult to make judgments in terms of R\({}_{\rm free}\). Accordingly, focusing on the specific radiation damage, the electron density maps of the disulfide bond regions of the four datasets were analyzed (Figure 6).