6QKN
Structure of the azide-inhibited form of cytochrome c peroxidase from obligate human pathogenic bacterium Neisseria gonorrhoeae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 110 |
| Detector technology | PIXEL |
| Collection date | 2016-06-01 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 79.120, 89.140, 94.830 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 64.950 - 2.300 |
| R-factor | 0.17336 |
| Rwork | 0.171 |
| R-free | 0.21461 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6fu3 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.907 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 65.000 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.117 | 0.723 |
| Number of reflections | 30270 | 2907 |
| <I/σ(I)> | 9.2 | |
| Completeness [%] | 97.7 | |
| Redundancy | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293 | 30 % 5/4 PO/OH and 0.1 M MES pH 6.0 in the presence of 2 mM CaCl2, 10 mM sodium ascorbate and 0.2 mM FMN |
