Table 1.
Data collection and refinement statistics
| SycT122 | |||
| native | crystal form #1 | crystal form #2 | |
| Data collection statistics | |||
| Space group | P21 | P212121 | P62 |
| Unit cell dimensions (Å), (°) | a=34.1, b=79.6, c=52.1 | a=51.5, b=63.1, c=74.4 | a=b=92.0, c=55.4 |
| α=γ=90, β=101.21 | α=β=γ=90 | α=β=90, γ=120 | |
| Data set | Peak | ||
| Wavelength (Å) | 1.05 | 0.9795 | 0.97957 |
| Resolution (Å) | 79.5–1.83 (1.86–1.83) | 48.1–2.0 (2.1–2.0) | 79.0–1.9 (2.0–1.9) |
| Mosaicity (°) | 0.5 | 0.25 | 0.14 |
| Completeness (%) | 97.6 (83.5) | 98.4 (96.4) | 99.5 (96.4) |
| (Anomalous) redundancy | 2.8 | 3.9 | 5.8 |
| Observations | 65,888 | 118,050 | 237,251 |
| Unique reflections | 23,529 | 16,331 | 21,134 |
| I/σ (I) | 14.8 (2.1) | 12.3 (4.6) | 16.6 (5.4) |
| Rsym, Rmeas | 5.6 (31.6)a | 8.0 (37.3)b | 7.2 (39.8)b |
| Phasing | Molecular replacement | Molecular replacement | SAD (selenium) |
| Number of sites | 6 sites in a dimer | ||
| Molecules per asymmetric unit | 2 | 2 | 2 |
| Solvent content (%) | 46 | 41 | 45 |
| Refinement statistics | |||
| R / Rfreec (%) | 18.4 / 23.3 | 21.9 / 28.4 | 19.6 / 23.6 |
| Atoms protein/solvent | 2131 / 504 | 1950 / 358 | 1908 / 477 |
| RMSD | |||
| Bonds (Å) / Angles (°) | 0.015 / 1.5 | 0.018 / 1.85 | 0.019 / 1.98 |
| Ramachandran plot | |||
| Residues in allowed / additionally allowed / generously allowed regions (%) | 94.1 / 5.9 / 0.0 | 86.1 / 13.5 / 0.5 | 88.2 / 10.4 / 1.4 |
| Residues in disallowed regions (%) | 0.0 | 0.0 | 0.0 |
| B factor (Å2) average / Wilson B | 28.2 / 28.5 | 20.6 / 31.6 | 32.2 / 32.1 |
| Protein / solvent | 27.8 / 33.8 | 21.0 / 26.2 | 31.0 / 40.5 |
Values in parentheses are for the highest resolution shell.
aRsym = 100 ∑n (∑i|Ii − Î|)/∑n (∑Ii).
b Rmeas = 100 n∑l |Î − Ii|/∑hkl (n − 1) ∑iIi, where Î is the mean intensity of symmetry-related reflections (Diederichs and Karplus 1997).
c R = 100 ∑hkl |Fobs − Fcalc| ∑hkl Fobs. Test set size 5%.