Table 1.
Table X-ray diffraction data collection and refinement statistics a
| Data collection | Form I | Form II |
|---|---|---|
| Space group | C2 | C2 |
| Cell dimensions | ||
| a, b, c (Å) | 501.0, 276.3, 161.0 | 223.7, 283.0, 160.8 |
| alpha,beta,gamma (°) | 90.00, 106.8, 90.00 | 90.0, 133.9, 90.0 |
| Resolution (Å) | 50.0-3.80 (3.94-3.80) | 50.0-3.70 (3.90-3.70) |
| Rmergeb | 0.181 (0.390) | 0.117 (0.476) |
| I/σ | 9.0 (1.6) | 7.4 (2.3) |
| Completeness (%) | 97.0 (81.4) | 99.5(99.4) |
| Redundancy | 3.2 (2.5) | 3.2 (3.3) |
| Refinement | ||
| Resolution (Å) | 50.0-3.80 | 50.0-3.70 |
| No. reflections | 199,545 | 76576 |
| Rwork/Rfree (%)c | 36.5/37.1 | 27.7/28.3 |
| No. atoms | ||
| Protein (one subunit) | 3849 | 3849 |
| Ligand/ion (ADP) | — | 27 |
| B-factors (Å2) | ||
| Equator domain | 70.4 | 108.5 |
| Median domain | 108.1 | 135.0 |
| Apical domain | 112.0 | 137.2 |
| Lid domain | 118.8 | 147.1 |
| r.m.s. deviations | ||
| Bond lengths (Å) | 0.01 | 0.01 |
| Bond angles (°) | 1.41 | 1.48 |
a
Corresponding parameters for the highest-resolution shell are shown in parentheses.
b
Rmerge =ΣhΣi|Iih −<Ih>| / ΣhΣi<Ih>, where <Ih> is the mean intensity of the observation Iih reflection h.
c
Rwork =Σ(‖Fp(obs)| − |Fp(calc)‖) / Σ|Fp(obs)|; Rfree = R factor for a selected subset (5%) of the reflections that was not included in prior refinement calculations.