Table 2.
Data collection and refinement statistics (molecular replacement)
| Mb(Lck_3)/Lck SH2 | Mb(Lck_1)/Lck SH2 | Mb(Yes_1)/Yes SH2 | |
|---|---|---|---|
| Data collection | |||
| Space group | P41212 | P3221 | I4122 |
| Cell dimensions | |||
| a, b, c (Å) | 81.83, 81.83, 105.96 | 91.40, 91.40, 88.78 | 101.86, 101.86, 139.62 |
| α, β, γ (°) | 90.00, 90.00, 90.00 | 90.00, 90.00, 120.00 | 90.00, 90.00, 90.00 |
| Resolution (Å) | 40.92–2.40 (2.49–2.40)⁎ | 45.70–2.85 (2.95–2.85)⁎ | 50.00–1.95 (1.98–1.95)⁎ |
| Rmerge | 3.0 (76.6) | 6.2 (1.0) | 0.13 (0.00) |
| I/σI | 37.91 (2.90) | 23.79 (1.63) | 24.44 (1.50) |
| Completeness (%) | 100.0 (99.00) | 100.0 (100.0) | 99.8 (99.7) |
| Redundancy | 7.2 (7.5) | 5.5 (5.7) | 19.1 (16.1) |
| Refinement | |||
| Resolution (Å) | 2.40 | 2.85 | 1.95 |
| No. of reflections | 14,544 | 10,316 | 27,104 (2649) |
| Rwork/Rfree | 0.20/0.25 | 0.23/0.27 | 0.19/0.22 |
| No. of atoms | |||
| Protein | 1555 | 1424 | 1652 |
| Ligand/ion | 2 | 15 | 33 |
| Water | 32 | – | 240 |
| B-factors | |||
| Protein | 68.40 | 79.67 | 33.18 |
| Ligand/ion | 63.77 | 115.24 | 46.73 |
| Water | 62.16 | – | 45.10 |
| rmsd | |||
| Bond lengths (Å) | 0.012 | 0.008 | 0.008 |
| Bond angles (°) | 1.16 | 1.31 | 0.84 |
⁎
One crystal for each structure.