TABLE 3.
Data collection and structure validation
| Data collection | |
| Wavelength (Å) | 0.9764 |
| Resolution (highest shell, Å) | 50.90-2.20 (2.26-2.20) |
| Space group | P43212 |
| Cell constants (Å) | a = 94.21, b = 94.21, c = 60.44, α = β = γ = 90° |
| Unique reflections | 14,286 (1043) |
| Average redundancy | 6.7 (6.8) |
| I/σ | 15.1 (2.3) |
| Completeness (%) | 99.8 (99.9) |
| Anomalous complete (%)a | 99.8 (100) |
| Rmergeb | 0.084 (0.604) |
| SAD phasing statistics | |
| Selenium ions per assymetric unit | 2 |
| Figure of merit (SOLVE 2.8 Å) | 0.35 |
| Figure of merit (RESOLVE 2.8 Å) | 0.66 |
| Refinement | |
| Rfactor | 20.45 |
| Rfree | 22.22 |
| r.m.s.d. bonds (Å) / angles (°) | 0.011/1.283 |
| B-factor deviationc | |
| Bonds/angles (Å2): | |
| Main chain | 0.729/1.118 |
| Side chains | 1.832/2.845 |
| Residues in Ramachandran cored (%) | 98.39 (1.61% in allowed regions) |
| Protein atoms | 1029 |
| Water atoms | 71 |
| Average B-factor (Å2) | 40.12 |
| Protein Data Bank accession code | 3MY2 |
| Molprobity score | 95th percentile |
a Anomalous completeness corresponds to the fraction of possible eccentric reflections generated from the anomalous diffraction in the dataset for which an anomalous difference has been measured. The anomalous completeness is the percent of the reflections in the dataset.
b Rmerge = Σhkl Σ|Ii − <I>|/Σhkl ΣiIi, where Ii is an intensity for the ith measurement of a reflection with indices hkl and <I> is the weighted mean of the reflection intensity.
c Isotropic thermal factor restraints.
d There are two residues, Lys162 and Gly113, that are not at the core of the Ramachandran plot, but they are in allowed regions.