Table 1.
Data collection and refinement statistics
| Crystal | SaCwlT (4fdy) | CdCwlT (4hpe) | ||
| Data collection | ||||
| Beamline | SSRL 11-1 | SSRL 12-2 | ||
| Space group | P21 | P1 | ||
| Data | λ1 MADSe | λ2 MADSe | λ3 MADSe | λ1 SADSe |
| Wavelength (Å) | 0.9790 | 0.9184 | 0.9785 | 0.9794 |
| Resolution range (Å) | 47.0-2.23 | 47.0-2.33 | 47.0-2.41 | 49.4-2.38 |
| No. of observations | 114,923 | 97,941 | 91,693 | 293,405 |
| No. of unique reflections | 33,428 | 28,768 | 26,611 | 76,631 |
| Completeness (%)a | 95.4 | 93.7 (83.5) | 95.8 (95.2) | 87.6 (84.5) |
| Mean I/σ (I)a | 12.9 (1.8) | 14.0 (2.2) | 19.2 (2.2) | 9.0 (2.3) |
| Rmerge on Ia (%) | 5.2 (68) | 5.0 (49) | 4.9 (56) | 10.9 (58) |
| Rmeas on Ia (%) | 6.2 (80) | 6.0 (59) | 5.8 (66) | 12.8 (68) |
| Rpim on Ia (%) | 3.3 (42) | 3.2 (31) | 3.1 (35) | 6.5 (34) |
| Highest resolution shell | 2.35-2.23 | 2.46-2.33 | 2.54-2.41 | 2.51-2.38 |
| Model and refinement statistics | ||||
| Data used in refinement | λ1 MADSe | λ1 SADSe | ||
| No. of reflections (total) | 33,396 | 76,620 | ||
| No. of reflections (test) | 1677 | 3897 | ||
| Cutoff criteria | |F|>0 | |F|>0 | ||
| Rcryst (%) | 19.9 | 17.6 | ||
| Rfree (%) | 24.2 | 21.1 | ||
| Stereochemical parameters | ||||
| Restraints (RMSD observed) | ||||
| Bond lengths (Å) | 0.010 | 0.010 | ||
| Bond angles (°) | 1.04 | 1.03 | ||
| MolProbity all atom clash score | 7.2 | 4.3 | ||
| Ramachandran plot (%)b | 97.1 (0) | 97.7 (0) | ||
| Rotamer outlier (%) | 1.4 | 0.6 | ||
| Average isotropic B-value (Å2)c | 65.5 (53.5) | 50.1 (48.9) | ||
| ESU based on Rfree (Å) | 0.21 | 0.22 | ||
| No. protein residues / chains | 590/2 | 1735/6 | ||
| Non-protein entities | 201 H2O | 590 H2O, 4 GOL, 9 CL | ||
Highest resolution shell in parentheses.
Percentage of residues in favored regions of Ramachandran plot (No. outliers in parenthesis).
This value represents the total B that includes TLS and residual B components (Wilson B-value in parenthesis). The average B-values of the protein and the solvents included in the refinement are very similar.
ESU = Estimated Standard Uncertainty in coordinates.
Rmerge=ΣhklΣi|Ii(hkl)-<I(hkl)>|/ΣhklΣiIi(hkl), Rmeas(redundancy-independent Rmerge) = Σhkl[Nhkl/(Nhkl-1)]1/2Σi|Ii(hkl)-<I(hkl)>|/ΣhklΣiIi(hkl), and Rpim(precision-indicating Rmerge)=Σhkl[1/(Nhkl-1)]1/2Σi|Ii(hkl)-<I(hkl)>|/ΣhklΣiIi(hkl).
Rcryst =Σ| |Fobs|-|Fcalc| |/Σ|Fobs|, where Fcalc and Fobs are the calculated and observed structure factor amplitudes, respectively.
Rfree = as for Rcryst, but for 5.0% of the total reflections chosen at random and omitted from refinement.