Table 1.
Data collection and refinement statistics
| ADP⋅BeFx | AMPPNP | ATP-γ-S-p-PDM | ADP-p-PDM | Nucleotide-free | |
|---|---|---|---|---|---|
| Data collection | |||||
| Resolution range, Å | 30.0–2.3 | 40.0–3.0 | 40.0–3.8 | 55.0–2.8 | 50–3.2 |
| Unique reflections/multiplicity | 49,703/4.4 | 31,019/3.5 | 14,451/3.0 | 30,488/2.0 | 20,298/4.2 |
| Average I/σ | 12.0 | 11.7 | 10.6 | 16.0 | 11.2 |
| Rsym, % (All/outer shell*) | 9.7/24.7 | 7.7/47.2 | 8.4/27.4 | 3.5/15.3 | 10.9/33.5 |
| Completeness (%): | |||||
| All data/outer shell* | 79.8/72.7 | 80.6/53.7 | 84.6/45.1 | 74.4/22.4 | 88.5/65.8 |
| 55–3.4 Å range | 90.7 | 93.1 | – | 95.0 | 93.0 |
| Refinement | |||||
| Sigma cutoff | 0.0 | 1.0 | 0.0 | 0.0 | 0.0 |
| Completeness in range, % | 77.9 | 73.1 | 78.8 | 72.0 | 84.1 |
| R factor/Rfree, % | 23.0/26.9 | 27.7/31.7 | 23.8/32.8 | 28.0/32.7 | 25.8/31.3 |
| Mean B factor | 55.8 | 79.1 | 53.4 | 89.8 | 84.1 |
| rms bond lengths, Å/angles, °† | 0.010/1.46 | 0.015/2.51 | 0.011/1.77 | 0.010/1.93 | 0.008/1.54 |
| No. of protein/water atoms | 8,476/185 | 8,237/7 | 8,069/6 | 8,282/31 | 8,127/10 |
| No. of prosthetic atoms | 40 | 34 | 34 | 30 | 8 |
| Cross-validated coordinate error, Ň | 0.41 | 0.64 | 0.69 | 0.67 | 0.49 |
The cell parameters of these 5 crystal structures are ADP⋅BeFx (P1: a = 51.6, b = 58.5, c = 133.3 Å, α = 81.1°, β = 84.9°, γ = 67.2°); AMPPNP (P1: a = 52.4, b = 58.6, c = 148.9 Å, α = 81.6°, β = 82.4°, γ = 87.4°); ATP-γ-S-p-PDM (P1: a = 51.8, b = 57.0, c = 151.7 Å, α = 95.2°, β = 96.5°, γ = 100.9°); ADP-p-PDM (P1: a = 51.8, b = 57.0, c = 150.5 Å, α = 95.6°, β = 96.3°, γ = 101.5°); and nucleotide-free near-rigor (P21: a = 159.8, b = 51.2, c = 84.0 Å, α = 90.0°, β = 99.5°, γ = 90.0°).
*
Highest resolution shell (10% of the theoretical data).
†
See ref. 36.