Table 1.
Data collection and refinement statistics (molecular replacement)
| 2-Allo | 1-Allo | 0-Allo | |
|---|---|---|---|
| Data collection | |||
| Space group | I 2 2 2 | P 21 21 2 | C 1 2 1 |
| Cell dimensions | |||
| a, b, c (Å) | 85.68, 102.78, 145.80 | 112.01, 130.25, 90.90 | 164.66, 109.92, 162.12 |
| α, β, γ (°) | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 | 90.0, 105.8, 90.0 |
| Resolution (Å) | 50–3.50 (3.56–3.50) | 50–3.40 (3.46–3.40) | 50–3.50 (3.56–3.50) |
| Rsym or Rmerge | 0.15 (0.71) | 0.14 (1.00) | 0.15 (1.00) |
| Mean I/σI | 19.6 (2.0) | 10.7 (1.5) | 6.4 (1.4) |
| Completeness (%) | 98.0 (98.8) | 98.9 (99.9) | 98.8 (98.9) |
| Redundancy | 4.2 (4.3) | 3.6 (3.6) | 2.4 (2.3) |
| CC1/2 | 0.54 | 0.43 | 0.53 |
| Refinement | |||
| Resolution (Å) | 20–3.50 (3.56–3.50) | 20–3.40 (3.46–3.40) | 20–3.50 (3.56–3.50) |
| No. of reflections | 8255 (796) | 18,591 (925) | 35,255 (1777) |
| Rwork/Rfree | 24.2/29.3 (36.0/35.4) | 19.2/24.5 (28.8/37.3) | 24.2/27.1 (32.3/34.5) |
| No. of atoms | |||
| Protein | 4131 | 8271 | 16,514 |
| Ligand/ion | 94 | 64 | 4 |
| Water | NA | 20 | 63 |
| B-factors | |||
| Protein | 122 | 98 | 89 |
| Ligand/ion | 114 | 88 | 72 |
| Water | NA | 44 | 35 |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.013 | 0.008 | 0.009 |
| Bond angles (°) | 1.4 | 1.1 | 1.2 |
One crystal for 2-Allo, 1-Allo, and 0-Allo structures was used for data collection and structure determination. Values in parentheses are for highest-resolution shell