Table 1.
Data collection, phasing, and refinement statistics.
| SeMet αMACPF-γ | αMACPF-γ | ||
|---|---|---|---|
| Space group | P21212 | P21212 | |
| Unit cell | a=95.4Å | a=96.6Å | |
| b=124.3Å | b=126.1Å | ||
| c=50.6Å | c=51.9Å | ||
| α=β=γ=90° | α=β=γ=90 | ||
| Data collection | |||
| Structure solution protocol | SAD | MR | |
| Wavelength (Å) | 0.9794 | 0.9565 | |
| Resolution (Å) | 50.0-2.3 | 50.0-2.15 | |
| Highest resolution shell (Å) | 2.32-2.30Å | 2.21-2.15 | |
| Unique reflections | 25296 | 30735 | |
| Redundancy | 4.9 (2.2) | 4.0 (3.0) | |
| Completeness (%) | 93.5 (53.1) | 91.9 (77.1) | |
| I/σ(I) | 13.9 (1.1) | 17.2 (2.4) | |
| Rmerge (%) | 12.7 (58.7) | 4.6 (33.4) | |
| SAD analysis | |||
| No. of Se sites located/theoretical | 11/13 | NA | |
| FOMMLPHARE | 0.23 | NA | |
| FOMDM | 0.73 | NA | |
| Refinement | |||
| Resolution range (Å) | 50.0-2.15 | ||
| No. protein atoms/AU | 3916 | ||
| No. waters/AU | 163 | ||
| R/Rfree (%) | 20.8/26.1 (30.0/42.3) | ||
| Mean B-factor (Å2) | overall | 45.7 | |
| Protein chain A | 53.0 | ||
| Protein chain C | 43.7 | ||
| Water molecules | 51.5 | ||
| RMSD bond length (Å) | 0.008 | ||
| RMSD angles (°) | 1.2 | ||
| Ramachandran favored (%) | 91.6 | ||
| Ramachandran allowed (%) | 8.2 | ||
| Ramachandran generously allowed (%) | 0.2 | ||
Values in parentheses correspond to the highest resolution shell
NA - not applicable
AU – asymmetric part of the unit cell