Table 1.
Data collection and refinement statistics
| PCH-2 SeMet | PCH-2 native | |
|---|---|---|
| Data collection | ||
| Synchrotron/Beamline | APS 24ID-E | SSRL 12-2 |
| Resolution (Å) | 3.23 | 2.3 |
| Wavelength (Å) | 0.97921 | 0.9795 |
| Space group | C2221 | C2221 |
| Unit cell dimensions (a, b, c) Å | 126.1, 239.5, 198.2 | 126.7 241.0 197.9 |
| Unit cell angles (α, β, γ) ° | 90, 90, 90 | 90, 90, 90 |
| I/σ (last shell) | 9.3 (1.0) | 17.9 (0.8) |
| * Rsym (last shell) | 0.198 (2.166) | 0.098 (3.143) |
| † Rmeas (last shell) | 0.213 (2.326) | 0.102 (3.297) |
| ‡ Isotropic CC1/2, last shell | 0.592 | 0.275 |
| § Directional CC1/2, last shell (Å) | ||
| a* | – | 0.498 (2.3 Å) |
| b* | – | 0.532 (2.3 Å) |
| c* | – | 0.608 (3.2 Å) |
| Completeness (last shell) % | 99.9 (99.9) | 99.5 (90.8) |
| Number of reflections | 33,462 | 1,808,343 |
| unique | 4410 | 134,133 |
| Multiplicity (last shell) | 7.5 (7.6) | 13.5 (10.6) |
| Number of sites | 68 | – |
| § Anisotropic scaling B-factors (Å2) | ||
| a* | – | −8.09 |
| b* | – | −8.02 |
| c* | – | 16.11 |
| isotropic B-factor correction | – | −19.65 |
| Refinement | ||
| Resolution range (Å) | – | 40 - 2.3 |
| No. of reflections | – | 96,084 |
| working | – | 91,200 |
| free | – | 4884 |
| # Rwork (%) | – | 22.97 |
| # Rfree (%) | – | 26.42 |
| Structure/Stereochemistry | ||
| Number of atoms | – | 18,017 |
| ligands (ADP, SO4) | – | 89 |
| solvent | – | 55 |
| r.m.s.d. bond lengths (Å) | – | 0.004 |
| r.m.s.d. bond angles (°) | – | 0.730 |
| ¶ PDB ID | – | 4XGU |
Rsym = ∑∑j|Ij − 〈I〉|/∑Ij, where Ij is the intensity measurement for reflection j and 〈I〉 is the mean intensity for multiply recorded reflections.
Rmeas = ∑h [√(n/(n − 1)) ∑j [Ihj − 〈Ih〉]/∑hj 〈Ih〉 where Ihj is a single intensity measurement for reflection h, 〈Ih〉 is the average intensity measurement for multiply recorded reflections, and n is the number of observations of reflection h.
CC1/2 is the Pearson correlation coefficient between the average measured intensities of two randomly-assigned half-sets of the measurements of each unique reflection (Karplus and Diederichs, 2012).
High-resolution native data were anisotropically scaled and elliptical data cutoffs were applied according to directional intensity and CC1/2 data (see ‘Materials and methods’ and Figure 3—figure supplement 1A for details on data anisotropy and resolution cutoffs).
Rwork, free = ∑||Fobs| − |Fcalc||/|Fobs|, where the working and free R-factors are calculated using the working and free reflection sets, respectively.
Coordinates and structure factors have been deposited in the RCSB Protein Data Bank (www.pdb.org).