Table 1.
Data collection and refinement statistics
Numbers in parentheses represent the value for the highest resolution shell. RMSD, root mean square deviation.
| Data collection and processing | |
| Source | SSRF-BL19U1 |
| Wavelength (Å) | 0.97538 |
| Space group | P212121 |
| Unit cell | |
| a, b, c (Å) | 35.513, 51.958, 136.984 |
| α, β, γ (degrees) | 90, 90, 90 |
| Resolution range (Å) | 50.00–2.10 (2.14–2.10) |
| No. of unique reflections | 14,123 (484) |
| Redundancy | 4.3 (2.5) |
| I/σ (I) | 11.3 (2.0) |
| Completeness (%) | 92.2 (65.2) |
| Rmerge (%)a | 10.4 (42.2) |
| Wilson B | 27.1 |
| Structure refinement | |
| Resolution (Å) | 41.39–2.11 (2.19–2.11) |
| Rworkb/Rfreec (%) | 18.04 (20.93)/24.56 (26.20) |
| RMSD bonds (Å)/angles (degrees) | 0.013/1.21 |
| No. of reflections | |
| Working set | 12,160 (553) |
| Test set | 601 (25) |
| No. of protein atoms | 2048 |
| No. of solvent atoms | 98 |
| Average B factor protein/peptide (Å2) | 32.64/33.30 |
| Ramachandran plot (%) | |
| Most favored regions | 97.4 |
| Additionally allowed | 2.6 |
| Generously allowed | 0 |
a Rmerge = ∑|Ii − Im|/∑Ii, where Ii is the intensity of the measured reflection, and Im is the mean intensity of all symmetry-related reflections.
b Rcryst = Σ‖Fobs| − |Fcalc‖/Σ|Fobs|, where Fobs and Fcalc are observed and calculated structure factors.
c Rfree = ΣT‖Fobs| − |Fcalc‖/ΣT|Fo|, where T is a test data set of about 5% of the total reflections randomly chosen and set aside before refinement.