Table 1.
Crystallographic data
| Data collection and phasing statistics | |||||
|---|---|---|---|---|---|
| Data set | λ1 | λ2 (edge) | λ3 (peak) | λ4 | Native |
| Anomalous statistics | Yes | Yes | Yes | Yes | No |
| Wavelength, Å | 0.9879 | 0.9793 | 0.9788 | 0.9668 | 1.000 |
| Resolution range, Å | 20.0–1.8 | 20.0–1.8 | 20.0–1.8 | 20.0–1.8 | 20.0–1.2 |
| Completeness (final shell)* | 97.4 (94.3) | 97.3 (94.7) | 97.3 (94.7) | 97.4 (94.4) | 93.6 (76.1) |
| Total no. of reflections | 147 797 | 146 841 | 147 191 | 147 914 | 137 483 |
| Unique no. of reflections* | 41 624 | 41 511 | 41 541 | 41 612 | 68 270 |
| Rsym (final shell), % | 2.8 (8.7) | 2.8 (7.2) | 2.8 (7.7) | 2.8 (8.2) | 4.7 (27.4) |
| I/σ(I) | 30.1 (12.9) | 32.9 (16.4) | 32.4 (16.3) | 30.4 (15.7) | 14.0 (2.6) |
| Phasing power, disp./anom.† | 1.7/2.3 | 1.6/4.1 | 1.1/4.8 | /3.5 | |
| RCullis, disp./anom.† | 0.66/0.58 | 0.64/0.39 | 0.74/0.34 | /0.43 | |
| f′ obs/f" obs | −4.3/0.6 | −6.7/3.9 | −5.3/3.9 | −3.8/2.5 | |
| Refinement statistics (based on all data, 1684 protein atoms and 193 solvent atoms) |
| B factors | Resolution range, Å | R, % | Rfree, % | rms
deviation
|
Bave Main/side/protein/solvent, Å | |
|---|---|---|---|---|---|---|
| Bonds, Å | Angles | |||||
| Isotropic | 20.0–1.2 | 21.8 | 23.0 | 0.013 | 1.6° | 11.0/13.7/12.3/21.5 |
| Anisotropic | 10.0–1.2 | 15.8 | 19.1 | 0.012 | 0.031 Å | 13.3/18.0/15.6/28.0 |
*
A Friedel pair is considered as two unique reflections for the anomalously processed data sets but as a single unique reflection for the nonanomalously processed data set.
†
40,865 structure factors were phased with a figure of merit of 0.79.