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 |