Table 1. Data collection and refinement statistics.
| SYCP1 αN-end 101-206 Open conformation (PDB 6F62) |
SYCP1 αN-end truncated 101-175 Closed conformation (PDB 6F5X) |
SYCP1 αC-end 676-770 Crystal form 1 (PDB 6F63) |
SYCP1 αC-end 676-770 Crystal form 2 (PDB 6F64) |
|
|---|---|---|---|---|
| Data collection | ||||
| Space group | 12 | 1222 | C2 | I4122 |
| Cell dimensions | ||||
| a, b, c (Å) | 65.67, 37.31, 108.52 | 28.64, 39.38, 165.77 | 233.42, 42.85, 43.69 | 43.38, 43.38, 292.18 |
| α β γ (°) | 90.00, 106.66, 90.00 | 90.00, 90.00, 90.00 | 90.00, 93.61, 90.00 | 90.00, 90.00, 90.00 |
| Wavelength (Å) | 0.9282 | 1.7712 | 0.9795 | 0.9795 |
| Resolution (Å) | 34.87–2.06 (2.12–2.06)a | 41.44–1.91 (1.95–1.91)a | 116.48–2.15 (2.27–2.15)a | 42.91–2.48 (2.58–2.48)a |
| Rmerge | 0.071 (0.919) | 0.028 (0.678) | 0.052 (0.695) | 0.080 (2.567) |
| Rpim | 0.023 (0.286) | 0.017 (0.541) | 0.032 (0.429) | 0.023 (0.727) |
| I / σ(I) | 15.0 (1.8) | 27.9 (1.8) | 12.4 (1.9) | 14.8 (1.5) |
| CC1/2 | 0.999 (0.969) | 1.000 (0.839) | 0.998 (0.872) | 1.000 (0.935) |
| Completeness (%) | 99.9 (100.0) | 99.3 (92.1) | 97.4 (88.0) | 99.8 (99.7) |
| Redundancy | 11.0 (11.4) | 5.9 (3.7) | 3.6 (3.5) | 13.2 (13.2) |
| Refinement | ||||
| Resolution (Å) | 27.23–2.07 | 41.44–1.91 | 58.26–2.15 | 39.63–2.49 |
| UCLA anisotropy (Å) | 2.1, 2.1, 2.6 | 1.9, 2.0, 2.1 | 2.2, 2.3, 2.2 | 2.9, 2.9, 2.5 |
| No. reflections | 12467 | 6754 | 21416 | 4138 |
| Rwork / Rfree | 0.2264/0.2441 | 0.2272/0.2392 | 0.2186/0.2526 | 0.2251/0.2517 |
| No. atoms | 1866 | 677 | 3318 | 806 |
| Protein | 1744 | 633 | 3143 | 786 |
| Ligand/ion | 18 | 12 | 0 | 4 |
| Water | 104 | 32 | 175 | 16 |
| B-factors | 42.79 | 58.4 | 46.97 | 60.86 |
| Protein | 42.51 | 57.7 | 47.30 | 60.80 |
| Ligand/ion | 62.91 | 83.9 | N/A | 81.59 |
| Water | 44.02 | 61.7 | 41.20 | 58.92 |
| R.m.s. deviations | ||||
| Bond lengths (Å) | 0.002 | 0.009 | 0.004 | 0.004 |
| Bond angles (°) | 0.334 | 1.020 | 0.511 | 0.575 |
a
Values in parentheses are for highest-resolution shell.