Table 1.
Data collection and structure refinement statistics.
| Parameter | Oxidized CnTrx1 |
|---|---|
| Data collection | |
| Wavelength (Å) | 1.2398 |
| Space group | P6422 |
| Cell dimensions (Å) | |
|
a, b, c α, β, γ |
110.706, 110.706, 91.761 90.00, 90.00, 120.00 |
| Resolution (Å)a | 25.00–1.80 (1.86–1.80) |
| Mosaicity (°) | 0.6 |
| No. of total reflections | 1,157,390 |
| No. of unique reflections | 31,224 |
| Redundancy | 37.1 (34.7) |
| Completeness (%) | 100.0 (100.0) |
| Rmergeb | 0.092 (0.581) |
| Rpimb | 0.015 (0.100) |
| CC1/2 | (0.976) |
| I/σ(I) | 53.9 (6.2) |
| Refinement | |
| Resolution (Å) | 25.00–1.80 |
| Model composition | |
| No. of protein residues | 105 |
| No. of water molecules | 347 |
| Ligands | 1 glycerol, 3 sulfate ions, 1 TRIS |
| Mean B-factor (Å2): all atoms | 37.27 |
| Rwork/Rfree | 0.155/0.198 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.023 |
| Bond angles (°) | 2.193 |
| Side chain double conformationc | Ile5A, Ser16A, Val20A, Val21A, Thr28A, Met35A,B, Ser37A, Lys42B, Met72A,B and Ile95B |
| PDB code | 5JY5 |
a
The values in parentheses refer to the highest resolution shell of 1.86–1.80 Å.
b
Rmerge = ∑hkl ∑i |Ii − <I>|/∑hkl ∑i Ii, Rpim = ∑hkl [1/(N-1)]1/2 ∑i |Ii − <I>|/∑hkl ∑i Ii where Ii is the intensity of a reflection i of the group represented by the unique reflection hkl, and <I> is the average intensity of the group represented by reflection hkl, and N is the total number of reflections in the hkl group.
c
Capital letters in superscript indicate the monomer.