6NAH
Crystal structure of Neisseria meningitidis ClpP protease in complex with Acyldepsipeptide-14 (ADEP-14)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E+ SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-03-15 |
| Detector | RIGAKU SATURN A200 |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 117.238, 195.976, 139.894 |
| Unit cell angles | 90.00, 97.42, 90.00 |
Refinement procedure
| Resolution | 49.631 - 2.700 |
| R-factor | 0.1928 |
| Rwork | 0.192 |
| R-free | 0.24790 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5dkp |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.444 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.11.1_2575)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.750 |
| High resolution limit [Å] | 2.020 | 2.700 |
| Rmerge | 0.920 | |
| Rmeas | 1.070 | |
| Rpim | 0.543 | |
| Number of reflections | 168533 | 8280 |
| <I/σ(I)> | 7.6 | |
| Completeness [%] | 98.7 | |
| Redundancy | 3.8 | |
| CC(1/2) | 0.559 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 294 | 0.2 M potassium thiocyanate 40% MPD |
