Table 1. Data collection and refinement statistics.
| apo-TkoTrm11 | TkoTrm11–SAM | SeMet I291M | |
|---|---|---|---|
| Data collection | |||
| Wavelength (Å) | 1.0000 | 1.0000 | 0.9791 |
| Space group | P212121 | P212121 | P212121 |
| Cell dimensions | |||
| a, b, c (Å) | 47.73, 53.52, 134.86 | 47.60, 53.79, 134,75 | 47.65, 53.81, 134,84 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Resolution (Å) | 50–1.70 (1.73–1.70) | 50–1.74 (1.80–1.74) | 50–1.75 (1.76–1.70) |
| Rmergea | 5.1 (59.4) | 4.3 (21.7) | 10.1 (33.8) |
| I / σI | 53.7 (4.2) | 41.6 (6.7) | 106.7 (15.5) |
| Completeness (%) | 99.8 (100.0) | 99.7 (99.3) | 100.0 (100.0) |
| Redundancy | 7.1 (7.2) | 5.1 (5.1) | 29.0 (28.0) |
| Refinement | |||
| Resolution (Å) | 34.4-1.70 | 32.6-1.74 | |
| No. reflections | 34,442 | 35,857 | |
| Rworkb/ Rfreec | 20.5/ 24.0 | 18.7/22.3 | |
| No. atoms | 2,774 | 2,909 | |
| Protein | 2,599 | 2,599 | |
| Water | 179 | 282 | |
| SAM | 0 | 1 | |
| Avg. B-factors (Å2) | 25.9 | 18.8 | |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.006 | 0.007 | |
| Bond angles (°) | 1.0 | 1.1 | |
| Ramachandran plot (%) | |||
| Most favored | 92.8 | 92.0 | |
| Additionally allowed | 6.9 | 7.6 | |
| Generously allowed | 0.0 | 0.0 | |
| Disallowed | 0.4 | 0.4 | |
The value in the parentheses is for the highest resolution shell.
aRmerge = ΣΣj|<I(h)> – I(h)j|/ΣΣj|<I(h)>|, where <I(h)> is the mean intensity of symmetry-equivalent reflections.
bRwork = Σ (IIFp(obs) – Fp(calc)II)/ΣIFp(obs)I.
cRfree = R factor for a selected subset (5%) of reflections that was not included in earlier refinement calculations.