Table 1. X-ray crystallographic data and final protein model refinement statistics for Diamond Light Source (DLS) data (refined in tetragonal and orthorhombic space groups) and Cu Kα data (orthorhombic).
Overall diffraction resolution values are given, with values for the outer diffraction resolution shell in parentheses.
| DLS (λ = 0.9763 Å) (tetragonal; PDB code 5nbj) | DLS (λ = 0.9763 Å) (orthorhombic)† | Cu Kα (λ = 1.5418 Å) (orthorhombic)† | |
|---|---|---|---|
| Data reduction | |||
| Space group | P43212 | P212121 | P212121 |
| Unit-cell parameters‡ (Å, °) | a = 79.89 (1), b = 79.89 (1), c = 37.00 (2), α = β = γ = 90 | a = 36.98 (3), b = 79.80 (1), c = 79.92 (1), α = β = γ = 90 | a = 79.70 (1), b = 79.71 (1), c = 36.83 (3), α = β = γ = 90 |
| Molecular mass (Da) | 14700 | 14700 | 14700 |
| Molecules per asymmetric unit | 1 | 2 | 2 |
| Detector | Dectris PILATUS 6M-F | Dectris PILATUS 6M-F | Bruker APEX II |
| Crystal-to-detector distance (mm) | 135 | 135 | 40 |
| X-ray wavelength (Å) | 0.97625 | 0.97625 | 1.5418 |
| Observed reflections | 735148 (31186) | 735464 (99591) | 647723 (22460) |
| Unique reflections | 32463 (1660) | 63838 (9126) | 22610 (3107) |
| Resolution (Å) | 39.95–1.27 | 56.47–1.26 | 39.86–1.79 |
| Completeness (%) | 99.9 (98.3) | 99.9 (99.5) | 99.4 (96.4) |
| R merge | 0.077 (2.066) | 0.077 (1.453) | 0.142 (0.750) |
| 〈I/σ(I)〉 | 20.9 (1.7) | 14.7 (1.6) | 17.52 (1.92) |
| Multiplicity | 22.6 (18.8) | 11.5 (10.9) | 28.48 (10.9) |
| Mn(I) half-set correlation CC1/2 | 0.999 (0.556) | 0.998 (0.536) | § |
| Cruickshank DPI (Å) | 0.049 | 0.050 | ¶ |
| Average B factor (Å2) | 21.0 | 22.8 | 20.45 |
| Refinement | |||
| R factor/R free (%) | 17.22/19.6 | 17.9/22.6 | 19.4/26.6 |
| R factor, all (%) | 17.22 | 18.2 | 16.6 |
| R.m.s.d., angles (°) | 1.145 | 2.793 | 1.122 |
| Ramachandran values (%) | |||
| Most favoured | 98.4 | 96.6 | 98.8 |
| Additional allowed | 1.56 | 3.44 | 1.16 |
| Disallowed | 0 | 0 | 0 |
The raw diffraction images are available at Zenodo (Brink & Helliwell, 2017 ▸).
Note that the order of the a, b, c unit-cell parameter values in Table 1 ▸ follows the respective conventions of the two different diffraction data-processing programs that we have used.
The CC1/2 metric is more recently introduced than the Bruker software used with the APEX II instrument, which therefore does not include it. The other, much used, metric of 〈I/σ(I)〉 crossing 2 is provided.
In the case of anisotropic protein model refinement undertaken at a diffraction resolution worse than ∼1.6 Å the calculated DPI formula denominator value of [number of observations (21313) − number of refined parameters (20690)] is approaching zero and the DPI estimate thus becomes unstable. Therefore, the distance values from our Cu Kα data cannot have reliably reported e.s.d. values. Details regarding the ‘DPI webserver’ can be found in Kumar et al. (2015 ▸). We prefer to use an anisotropic refinement for the Cu Kα case as it improved the F o − F o residual density, in particular around the Re atoms and their coordinated ligands.