3TI9
Crystal structure of the basic protease BprB 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 |
| Collection date | 2007-06-07 |
| Detector | RIGAKU RAXIS |
| Wavelength(s) | 1.542 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.462, 90.514, 44.060 |
| Unit cell angles | 90.00, 109.99, 90.00 |
Refinement procedure
| Resolution | 24.383 - 1.800 |
| R-factor | 0.1591 |
| Rwork | 0.157 |
| R-free | 0.20670 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.054 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 45.270 |
| High resolution limit [Å] | 1.800 |
| Number of reflections | 24768 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6.5 | 293 | PEG 1500, pH 6.5, vapor diffusion, temperature 293K |
