Table 1.
X-ray data collection, analysis and refinement statistics for the crystal structure of the PknH ECD.
| Data Collection | PknH ECD Tb3+ Complex |
|---|---|
| Wavelength (Å) | 1.12 |
| Temperature (K) | 100 |
| Space group | P21 |
| Unit cell parameters | |
| a, b, c (Å) | 47.46, 35.92, 49.31 |
| β(°) | 98.36 |
| Resolution (Å) a | 50.0-1.70 (1.76–1.70) |
| Number of unique reflections | 34200 (3328) |
| Rsym (%) | 6.1 (25.3) |
| I/σI | 17.4 (4.9) |
| Completeness (%) | 98.8 (98.1) |
| Redundancy | 3.8 (3.8) |
| SAD Solution | |
| Proteins per a.u. | 1 |
| Terbium Sites per a.u. | 2 |
| Mean figure of merit | 0.424 |
| Refinement | |
| Resolution (Å) | 48.78-1.70 |
| Number of reflections | 34190 |
| Rwork/Rfree (%) | 16.30 / 19.74 |
| Number of atoms | |
| Protein | 1467 |
| Solvent | 221 |
| Average B factors | |
| Protein (Å2) | 17 |
| Solvent (Å2) | 25 |
| Rmsd | |
| Bond lengths (Å) | 0.013 |
| Bond angles (°) | 0.96 |
| Ramachandran plot | |
| Favored (%) | 96 |
| Allowed (%) | 4 |
| PDB ID | 4ESQ |
Notes on Table 1: Data were collected at 100 K at Beamline 8.3.1 at the Lawrence Berkeley National Laboratory Advanced Light Source.39 Data were reduced and scaled with HKL2000.40 The structure was determined using PHENIX41 and the model was adjusted manually using Coot42. Phenix.autosol found two terbium sites per asymmetric unit, and phenix.autobuild produced a model with 191 residues and an Rfree of 24% after seven cycles of automatic building and refinement. Building and refinement were completed with phenix.refine and Coot and included addition of a single ordered molecule of BIS-TRIS buffer that coordinated one of the two terbium ions. The final model was validated using MolProbity.43