6FU3
Structure of the mixed-valence, active form, of cytochrome c peroxidase from obligate human pathogenic bacterium Neisseria gonorrhoeae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | BRUKER IMUS MICROFOCUS |
Temperature [K] | 110 |
Detector technology | CMOS |
Collection date | 2016-04-04 |
Detector | BRUKER PHOTON 100 |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 78.942, 88.780, 93.122 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 23.820 - 1.800 |
R-factor | 0.20946 |
Rwork | 0.208 |
R-free | 0.24360 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vhd |
RMSD bond length | 0.016 |
RMSD bond angle | 2.198 |
Data reduction software | PROTEUM |
Data scaling software | SAINT |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 64.300 | 1.820 |
High resolution limit [Å] | 1.790 | 1.790 |
Rmerge | 0.157 | 0.840 |
Number of reflections | 61589 | 2299 |
<I/σ(I)> | 10.3 | |
Completeness [%] | 99.1 | |
Redundancy | 9.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 278 | 30% 5/4 PO/OH and 0.1M MES pH6.0 in the presence of 2mM CaCl2, 10mM sodium ascorbate and 0.2mM FMN, using a 20mg/mL protein solution previously incubated with calcium, sodium ascorbate and FMN. |