Table 1. Crystallographic data collection, phasing and refinement statistics.
| PDB deposition code | 6TH1 | 6TGZ | |||
|---|---|---|---|---|---|
| Data collection | |||||
| Crystal | ratIE1 30–392 | SeMet ratIE1 30–392 | humIE1 14–382 | ||
| Space group | P6522 | C2221 | |||
| Cell dimensions | |||||
| a, b, c (Å) | 173.1, 173.1, 133.5 | 173.4, 173.4, 133.9 | 110.0, 134.1, 70.5 | ||
| α, β, γ (°) | 90.0, 90.0, 120.0 | 90.0, 90.0, 90.0 | |||
| Dataset | Native | 6 keVa,b | Peaka,c | Inflectiona | Native |
| Wavelength (Å) | 0.9184 | 2.0664 | 0.9797 | 0.9798 | 2.033 |
| Resolution (Å) | |||||
| Spherical | 20–3.4 (3.6–3.4)d | 20–5.0 (5.1–5.0) | 20–4.0 (4.1–4.0) | 20–4.0 (4.1–4.0) | 20–3.2 (3.3–3.2) |
| Ellipsoidal | 3.24 (a* direction) 3.29 (b* direction) 3.20 (c* direction) |
||||
| Rmeas (%) | 35.7 (605) | 11.4 (39.4) | 48.2 (202) | 40.2 (192) | 21.9 (150) |
| Rpim (%) | 3.9 (67.0) | n.d.e | n.d. | n.d. | 6.0 (40.6) |
| I/σ(I) | 19.2 (0.9) | 35.0 (13.7) | 14.0 (2.9) | 7.3 (1.8) | 8.4 (1.1) |
| CC1/2 (%) | 100.0 (29.5) | 100.0 (99.4) | 99.8 (80.1) | 99.6 (76.7) | 99.8 (79.2) |
| CC* (%) | 100 (67.5) | 100 (94.5) | |||
| Resolution limit anomalous signal (Å)f | n.d. | 5.0 | 5.0 | 6.0 | n.d. |
| Completeness (%) | |||||
| Spherical | 99.0 (97.2) | 98.4 (100.0) | 99.8 (98.5) | 99.9 (100.0) | 92.8 (63.6) |
| Ellipsoidal | 95.9 (88.7) | ||||
| Multiplicity | 80 | 72 | 90 | 21 | 13 |
| Refinement | |||||
| Resolution range (Å) | 20–3.4 (3.5–3.4) | 20–3.2 (3.3–3.2) | |||
| No. of unique reflections | 16608 | 8257 | |||
| Reflections used for Rfree | 1626 (158) | 800 (47) | |||
| Rwork (%) | 21.5 (35.4) | 22.5 (30.7) | |||
| Rfree (%) | 24.6 (37.0) | 26.8 (29.5) | |||
| CCwork (%) | 97.9 (53.6) | 93.8 (60.0) | |||
| CCfree (%) | 96.4 (64.0) | 94.9 (84.9) | |||
| Ramachandran (%) | |||||
| favored/outlier | 98.0/0.0 | 98.3/0.0 | |||
| Total no. of atoms | 2799 | 2807 | |||
| No. of protein atoms | 2799 | 2807 | |||
| B-factors (Å)2 | 130 | 54.8 | |||
| No. of TLS groups | 3 | 8 | |||
| R.m.s deviations | |||||
| Bond lengths (Å) | 0.004 | 0.005 | |||
| Bond angles (°) | 0.84 | 0.91 | |||
a Values calculated with the Friedel’s law equal false setting.
b Merged data from seven crystals.
c Merged data from five crystals.
d Values in parentheses refer to the highest resolution shell.
e not determined
f Defined as the resolution value where the correlation between anomalous differences drops below 30%. Values estimated from SHELXC [61].