3TI7
Crystal structure of the basic protease BprV from the ovine footrot pathogen, Dichelobacter nodosus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU RAXIS |
| Wavelength(s) | 1.542 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.497, 89.637, 47.654 |
| Unit cell angles | 90.00, 113.61, 90.00 |
Refinement procedure
| Resolution | 27.724 - 2.000 |
| R-factor | 0.166 |
| Rwork | 0.163 |
| R-free | 0.22550 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.153 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 44.810 |
| High resolution limit [Å] | 2.000 |
| Number of reflections | 20018 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6.5 | 293 | PEG 3350, pH 6.5, vapor diffusion, temperature 293K |
