TABLE 1.
Crystallographic statistics
| Data collection | |||||
|---|---|---|---|---|---|
| Data set | Native | Peak | Inflection | Remote | |
| Wavelength (Å) | 0.97921 | 0.97918 | 0.979291 | 0.97151 | |
| Cell dimensions (Å, degrees) | a = b = 71.9, c = 151.7, γ = 120 | a = b = 71.5, c = 153.0, γ = 120 | a = b = 71.3, c = 154.3, γ = 120 | a = b = 71.3, c = 153.4, γ = 120 | |
| Total reflections | 123,313 | 52,772 | 36,510 | 55,164 | |
| Unique reflections | 12,496 | 7727 | 3554 | 4844 | |
| Resolutiona (Å) | 48.1–1.88 (1.98–1.88) | 30.4–2.19 (2.31–2.19) | 48.2–2.88 (3.04–2.88) | 48.1–2.59 (2.73–2.59) | |
| R-mergea | 0.092 (0.536) | 0.058 (0.355) | 0.092 (0.326) | 0.061 (0.348) | |
| I/σ(I)a | 22.1 (4.4) | 16.8 (5.6) | 19.6 (5.5) | 22.5 (6.7) | |
| Completenessa (%) | 99.6 (97.2) | 97.2 (95.7) | 98.6 (93.1) | 98.6 (94.2) | |
| Redundancya | 9.9 (7.2) | 6.8 (7.0) | 10.3 (5.9) | 11.4 (11.3) | |
| Phasing/refinement | |||||
| Patterson figure of merit | 100.8 | ||||
| Resolution | 48.1–1.88 | ||||
| R-factor | 0.217 | ||||
| Rfree | 0.238 | ||||
| Number of protein atoms | 746 | ||||
| Number of solvent atoms | 42 | ||||
| Average B-factors (Å2) (TLS residuals) | 22.3 | ||||
| Protein atoms (Å2) | 21.5 | ||||
| Solvent atoms (Å2) | 29.1 | ||||
| r.m.s.d. bond lengths (Å2) | 0.016 | ||||
| r.m.s.d. bond angles (degrees) | 1.742 | ||||
| B-factor correlations (Å2) | 7.2 | ||||
a The values in parentheses indicate statistics for the highest resolution shell.