Table 1.
Crystallographic parameters, data collection and refinement statistics
| Native | Acetate complex | |
|---|---|---|
| Crystallographic parameters | ||
| Space group | P212121 | P212121 |
| Unit-cell dimensions (Å) | 43.43, 54.14, 121.41 | 43.03, 54.01, 120.71 |
| 90.0, 90.0, 90.0° | 90.0, 90.0, 90.0° | |
|
| ||
| Data collection statistics | ||
| Resolution limits (Å) | 32.6 – 1.51 | 35.0 – 1.35 |
| Number of observed reflections | 424975 | 326939 |
| Number of unique reflections | 44785 | 61823 |
| Completeness | ||
| overall/outer shell | 97.7/86.9 | 98.6/96.9 |
| Redundancy | ||
| overall/outer shell | 9.5/4.4 | 5.3/3.5 |
| Rsyma(%) | ||
| overall/outer shell | 5.1/44.3 | 6.7/48.6 |
| Rmrgd-Fb(%) | ||
| overall/outer shell | 6.8/48.7 | 8.5/57.0 |
| I/σ | ||
| overall/outer shell | 26.7/3.4 | 15.7/2.8 |
|
| ||
| Refinement statistics | ||
| Resolution limits | 32.6 - 1.51 | 35.0 – 1.35 |
| Number of reflections/% | 42520/97.7 | 58636/98.6 |
| Reflections used for Rfree | 2258 | 3118 |
| R(working)c (%) | 16.2 | 16.1 |
| Rfreedd (%) | 18.2 | 17.4 |
| Model contents/average B (Å2) | ||
| Protein atoms | 2156/19.8 | 2167/15.1 |
| Ligand atoms | 0 | 0 |
| Ions/buffer atoms | 0 | 31/21.3 |
| Water molecules | 299/30.4 | 276/25.5 |
| Ramachandran favored/outliers | 99.6/0.0 | 99.6/0.0 |
| RMS deviations | ||
| Bond length (Å) | 0.016 | 0.016 |
| Bond angle (°) | 1.511 | 1.613 |
a
Rsym = Σ | Iavg − Ii|/Σ Ii
b
Rmrgd-F, refer to [32]
c
R(working) = Σ|Fp − Fpcalc |/ΣFp, where Fp and Fpcalc are observed and calculated structure factors
d
Rfree is calculated with 5% of the data.