7RQH
Crystal Structure of carboxyl-terminal processing protease A mutant S302A, CtpA_S302A, of Pseudomonas aeruginosa
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-08-16 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 1.07803 |
| Spacegroup name | H 3 |
| Unit cell lengths | 189.650, 189.650, 131.105 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 43.030 - 3.200 |
| R-factor | 0.2422 |
| Rwork | 0.241 |
| R-free | 0.26540 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7rpq |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.739 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.19_4092)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 94.820 | 3.370 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.089 | |
| Number of reflections | 28884 | 4245 |
| <I/σ(I)> | 15.6 | |
| Completeness [%] | 99.6 | 99.9 |
| Redundancy | 10.3 | 10.6 |
| CC(1/2) | 0.999 | 0.524 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4 | 293 | 0.1 M sodium acetate, pH 4.0, and 0.6 M ammonium dihydrogen phosphate at a concentration of 33 mg/mL |






