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. |
