TABLE 1.
X-ray diffraction data and atomic refinement for the CdiA-CT·CdiIE479 complex
NA means not applicable.
| Se-SAD dataset | Native dataset | |
|---|---|---|
| Space group | I4 | P22121 |
| Unit cell dimensions (Å) | 117.2 × 117.2 × 111.6 | 54.5 × 73.3 × 110.0 |
| pH of crystallization condition | 6.5 | 7.0 |
| Protein concentration (mg/ml) | 20 | 20 |
| Dataset | ||
| Wavelength, Å | 0.97591 | 0.97591 |
| Resolution range | 50–3.3 | 50–2.0 |
| Unique reflections (total) | 22,290 (329,892) | 30,121 (322,487) |
| Completeness, %a | 100 (100) | 99.24 (99.28) |
| Redundancya | 14.8 (14.9) | 10.7 (10.9) |
| Rmergea,b | 0.159 (0.48) | 0.071 (0.494) |
| Rmeasa,c | 0.157 (0.467) | 0.075 (0.519) |
| Rp.i.m. a,d | 0.041 (0.121) | 0.023 (0.156) |
| CC1/2a | 0.999 (0.993) | 0.998 (0.966) |
| I/σa | 18.03 (6.95) | 29.99 (5.79) |
| Figure of merit | 0.408 | NA |
| No. of selenium sites | 18 | NA |
| NCS copies | 3 | 2 |
| Model refinement | ||
| Resolution range, Å | 43.7–2.0 | |
| No. of reflections (working/free) | 30,094 | |
| No. of protein atoms | 3,382 | |
| No. of water molecules | 155 | |
| Residues in model | CdiA-CT 201–316; CdiI 2–105 | |
| Rwork/Rfree %e | 19.3/23.7 | |
| Room mean square deviations | ||
| Bond lengths, Å | 0.008 | |
| Bond angles | 1.09 | |
| Ramachandran plot | ||
| Most favorable region, % | 98.8 | |
| Additional allowed region, % | 1.2 | |
| Disallowed region | 0 | |
| PDB code | 5J4A | |
a Statistics for the highest resolution shell are given in parentheses.
b Rmerge = ΣhklΣi|Ii(hkl) − (I(hkl))|/ΣhklΣi Ii(hkl).
c Rmeas = Σhkl {N(hkl)/(N(hkl) − 1)}1/2 Σi|Ii(hkl) − (I(hkl))|/ΣhklΣi Ii(hkl).
d Rp.i.m (precision-indicating Rmerge) = Σhkl {1/(N(hkl) − 1)}½ Σi|Ii(hkl) − (I(hkl))|/ΣhklΣi Ii(hkl).
e Rwork = Σ|Fobs − Fcalc|/ΣFobs. Rfree was computed identically except where all reflections belong to a test set of 5% randomly selected data.