Table 3.
X-ray diffraction data collection and atomic refinement statistics for Mt-DsbA in its reduced form
| Space group | P21212 |
|---|---|
| No of monomers per AS unit |
2 |
| Unit cell dimensions (Å) |
71.0 × 76.7 × 86.9 |
| pH of crystallization condition |
7.4 |
|
Data set |
|
| Wavelength (Å) |
0.976 |
| Resolution range (Å) |
44.70-1.90 |
| Unique reflections (total) |
38372 (706287) |
| Completeness (%)¶ |
99.96 (100) |
| Redundancy |
10.7 (10.6) |
| Rmerge¶,a |
7.4 (39.3) |
| I/σ¶ |
5.8 (1.9) |
|
Model refinement |
|
| Resolution range (Å) |
44.70-1.90 |
| No. of reflections (working/free) |
36450/1922 |
| Residues of Mt-DsbA |
Chain A 56-255 |
| |
Chain B 49-255 |
| No. of protein atoms |
5975 |
| No. of water molecules |
300 |
|
Rwork/Rfreeb, % |
20.2/23.8 |
|
Ramachandran plot |
|
| Most favorable region (%) |
97.30 |
| Additional allowed region (%) |
2.21 |
| Disallowed region (%) |
0.49 |
| PDB ID code | 4IHU |
¶Statistics for the highest resolution shell are given in (parenthesis).
a Rmerge=Σ|I-<I>|/ΣI.
b Rwork=Σ|Fobs-Fcalc|/ΣFobsRfree was computed similarly for a test set of 5% randomly selected data, which were not used in refinement.