TABLE 1.
Data collection and refinement statistics
| Data collection | |
| Wavelength (Å) | 0.9184 |
| Resolution (Å)a | 35.12–1.8 (1.9–1.8) |
| Space group | P32 |
| Cell dimensions | |
| a = b, c (Å) | 70.2, 74.8 |
| α = β, γ (degrees) | 90, 120 |
| Unique reflections | 38,133 |
| 〈I/σ(I)〉a,b | 7.5 (2.4) |
| Completeness (%)a | 100 (100) |
| Redundancya | 3.8 (3.8) |
| Rsyma,c | 0.106 (0.492) |
| Refinement statistics | |
| Resolution limits | 35.12–1.8 |
| No. of reflections | 38,107 |
| No. of protein/ligand/solvent atoms | 2,902/4/381 |
| Rcryst (Rfree)d | 0.147 (0.171) |
| Root mean square deviations | |
| Bond lengths (Å) | 0.006 |
| Bond angles (degrees) | 1.057 |
| Average B-factors (Å2) | |
| Protein (p97N/gp78) | 32.2/32.8 |
| Solvent molecules | 39.0 |
| Ramachandran statistics (%)e | |
| Favored | 95.8 |
| Allowed | 3.9 |
| Outliers | 0.3 |
a Numbers in parentheses refer to the respective highest resolution data shell in the data set.
b 〈I/σI〉 indicates the average of the intensity divided by its S.D. value.
c Rsym = 
hkli|Ii − 〈I〉|/hkli〈I〉, where Ii is the ith measurement and 〈I〉 is the weighted mean of all measurements of I.
d Rcryst = ‖Fo| − |Fc‖/|Fo|, where Fo and Fc are the observed and calculated structure factor amplitudes. Rfree, same as Rcryst for 5% of the data randomly omitted from the refinement.
e Ramachandran statistics indicate the fraction of residues in the favored (98%), allowed (>99.8%), and disallowed regions of the Ramachandran diagram, as defined by MolProbity (45).