TABLE 1.
LigE and LigF statistics
Summary of crystal parameters, data collection, and refinement statistics. Values in parentheses are for the highest resolution shell.
| LigFΔ242-GSH | LigEΔ255 | LigEΔ255-GSH | |
|---|---|---|---|
| Crystal parameters | |||
| Space group | P6322 | C2 | C2 |
| Unit cell parameters | |||
| a, b, c (Å) | 123.71, 123.71, 66.42 | 122.55, 97.15, 131.38 | 121.00, 96.13, 126.16 |
| β | 106.65 | 81.52 | |
| Data collection statistics | |||
| Wavelength (Å) | 0.97857 | 0.999 | 1.000 |
| Resolution range (Å) | 50.00–2.07 (2.11–2.07) | 50–1.90 (1.93–1.90) | 50–2.6 (2.65–2.60) |
| No. of reflections (measured/unique) | 326,246/18,884 | 575,459/114,153 | 160,219/42,163 |
| Completeness (%) | 99.8 (98.3) | 99.2 (99.9) | 97.7 (93.8) |
| Rmergea | 0.076 (0.637) | 0.137 (0.63) | 0.135 (0.61) |
| Redundancy | 17.3 (12.9) | 5.0 (4.9) | 3.8 (3.6) |
| Mean I/σ(I) | 9.1 (3.8) | 9.0 (1.6) | 6.1 (2.5) |
| Refinement and model statistics | |||
| Resolution range (Å) | 40.49–2.07 (2.17–2.07) | 48–1.90 (1.95–1.90) | 48–2.60 (2.65–2.60) |
| No. of reflections (work/test) | 17,278/964 | 114,138/1,999 | 42,158/2,000 |
| Rcrystb | 0.161 (0.182) | 0.227 (0.289) | 0.222 (0.266) |
| Rfreec | 0.214 (0.263) | 0.271 (0.350) | 0.267 (0.290) |
| Root mean square deviation bonds (Å) | 0.008 | 0.004 | 0.003 |
| Root mean square deviation angles (degrees) | 1.022 | 0.956 | 0.776 |
| B factor (protein/solvent) (Å2) | 39.58/43.93 | 29.13/37.54 | 34.22/27.38 |
| B factor (GSH) (Å2) | 26 | 146, 148, 149, 146 | |
| No. of protein atoms | 1,983 | 9,405 | 8,491 |
| No. of waters | 229 | 1,159 | 165 |
| Auxiliary molecules (real space correlation coefficient (CC)) | 1 glutathione (0.97), 1 Tris (0.95), 1 PEG (0.95) | 4 glutathione (1 per chain, A = 0.71, B = 0.58, C = 0.58, D = 0.61) | |
| Ramachandran plot | |||
| Favorable region | 98.4 | 95.8 | 94.4 |
| Additional allowed region | 1.6 | 3.0 | 4.3 |
| Disallowed region | 0 | 1.2 | 1.3 |
| Protein Data Bank entry | 4XT0 | 4YAM | 4YAN |
a Rmerge = ΣhΣi|Ii(h) − 〈I(h)〉|/ΣhΣi Ii(h), where Ii(h) is the intensity of an individual measurement of the reflection, and 〈I(h)〉 is the mean intensity of the reflection.
b Rcryst = Σh‖Fobs| − |Fcalc‖/Σh|Fobs|, where Fobs and Fcalc are the observed and calculated structure factor amplitudes, respectively.
c Rfree was calculated as Rcryst using 5.0% of randomly selected unique reflections that were omitted from the structure refinement.