Table 1.
Crystallographic data collection and refinement statistics.
| Cleaved S-terminase | Full Length S-terminase | ||
|---|---|---|---|
| Native-gp3 | SeMet-gp3 | FL-gp3 | |
| Data collection | |||
| Space group | P21 | P21 | P21212 |
| Cell dimensions | |||
| a, b, c (Å) | 76.48, 100.90, 89.95 | 80.22, 101.18, 89.09 | 143.46, 144.93, 144.61 |
| α, β, γ (Å) | 90, 93.73, 90 | 90, 92.87, 90 | 90, 90, 90 |
| Wavelength (Å) | 0.99 | 0.97 | 0.97 |
| Resolution (Å) | 15–1.75 (1.81–1.75) | 20–2.5 (2.54–2.50) | 20–3.35 (3.42–3.35) |
| Reflections (tot/unique) | 2,483,158 / 126,076 | 7,505,096 / 49,292 | 747,842 / 43,496 |
| R sym | 7.1 (67.4) | 9.6 (30.8) | 17.5 (64.6) |
| I / σI | 28.2 (1.8) | 36.8 (9.0) | 14.7 (3.3) |
| Completeness (%) | 93.5 (62.5) | 99.8 (100.0) | 99.9 (99.7) |
| Redundancy | 4.4 (3.3) | 8.3 (8.1) | 5.7 (5.6) |
| Refinement | |||
| Resolution (Å) | 15–1.75 | 20–3.35 | |
| No. reflections | 126,076 | 41,398 | |
| Rwork / Rfreeb | 17.73 / 21.65 | 23.24 / 26.45 | |
| No. atoms | |||
| Protein | 11,158 | 19,348 | |
| Water | 1,397 | 0 | |
| B-factors (Å2) | |||
| Protein | 36.5 | 59 | |
| Water | 40.1 | ||
| R.m.s deviations | |||
| Bond lengths (Å) | 0.006 | 0.009 | |
| Bond angles (°) | 0.918 | 1.208 | |
*
Values in parentheses are for highest-resolution shells.
a
Rsym =Σi,h|I(i,h) − <I(h)>|/Σi,h|I(i,h)| where I(i,h) and <I(h)> are the ith and mean measurement of intensity of reflection h.
b
The Rfree value was calculated using 2,000 reflections selected randomly for native-gp3 and in thin resolution shells for Full Lenath S-terminase.