TABLE 1.
Data collection and refinement statistics for GrxS12·GSH and GrxS12·GSH·βMSH crystals
| Data set | GrxS12·GSH | GrxS12·GSH·βMSH |
|---|---|---|
| Data collection and processing statistics | ||
| Data collection site | X11 DESY/EMBL-Hamburg | X13 DESY/EMBL-Hamburg |
| Wavelength (Å) | 0.8150 | 0.8063 |
| Space group | P212121 | P212121 |
| Unit cell dimensions (Å) (a, b, c) | 39.03, 47.27, 55.62 | 38.83, 46.82, 55.36 |
| Asymmetric unit | 1 subunit | 1 subunit |
| Resolution range (Å)a | 50.00–1.70 (1.73–1.70) | 50.00–1.80 (1.86–1.80) |
| Redundancya | 4.49 (4.16) | 6.69 (6.85) |
| Completeness (%)a | 99.7 (95.0) | 99.6 (100.0) |
| I/σIa | 13.37 (2.26) | 23.26 (16.95) |
| Rmergea,b | 0.045 (0.239) | 0.048 (0.107) |
| Refinement statistics | ||
| Resolution range (Å) | 36.0–1.70 | 30.0–1.80 |
| Reflections used | 11,234 | 9301 |
| Rcrystc (Rfree)d | 19.28 (23.95) | 16.78 (21.45) |
| Protein/waters/GSH/HED | 106 residues/186/1/0 | 106 residues/186/1/0 |
| Mean B factor (Å2) | ||
| Main chain | 16.53 | 12.04 |
| Side chain | 23.33 | 14.79 |
| Water | 32.57 | 27.88 |
| Ligand | 15.31 | 17.00 |
| All | 20.52 | 16.24 |
| r.m.s. deviation from ideal geometry | ||
| Bond lengths (Å) | 0.012 | 0.011 |
| Bond angles (degrees) | 1.4 | 1.4 |
| Dihedral angles (degrees) | 23.5 | 23.7 |
| Improper angles (degrees) | 1.61 | 1.75 |
| Ramachandran plot | ||
| Residues in most favored regions (%) | 96.7 | 95.6 |
| Residues in additionally allowed regions (%) | 3.3 | 4.4 |
| Residues in generously allowed regions (%) | 0.0 | 0.0 |
a
Rcryst = Σ|Fo – Fc|/ΣFo, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively
b
The Rfree value was calculated from 5% of all data that were not used in the refinement
c
Rcryst = Σ|Fo – Fc|/ΣFo, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively
d
Rfree is as for Rcryst but calculated for a test set comprising reflections not used in the refinement (5%)