4C2D
Crystal structure of the protease CtpB in an active state
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 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 117.050, 65.375, 169.065 |
| Unit cell angles | 90.00, 95.03, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.700 |
| R-factor | 0.2271 |
| Rwork | 0.227 |
| R-free | 0.24130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4c2c |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.140 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.740 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.140 | 0.810 |
| Number of reflections | 79111 | |
| <I/σ(I)> | 12.6 | 2.1 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 6.8 | 6.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 13% PEG 3350, 0.1 M NA-MALONATE, 0.1 M HEPES PH 7.8 |
