3O3V
Crystal structure of ClbP peptidase domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-07-28 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9765 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 103.940, 149.930, 87.330 |
Unit cell angles | 90.00, 123.90, 90.00 |
Refinement procedure
Resolution | 19.940 - 2.400 |
R-factor | 0.20604 |
Rwork | 0.204 |
R-free | 0.24125 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.919 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.940 | 2.530 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.086 | 0.280 |
Number of reflections | 39793 | |
<I/σ(I)> | 11.5 | 3.7 |
Completeness [%] | 92.3 | 94.3 |
Redundancy | 3 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | potassium phosphate 1.2M, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |