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 |