5E0S
crystal structure of the active form of the proteolytic complex clpP1 and clpP2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-06-06 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 205.179, 183.541, 188.373 |
| Unit cell angles | 90.00, 94.53, 90.00 |
Refinement procedure
| Resolution | 49.270 - 2.900 |
| R-factor | 0.20499 |
| Rwork | 0.204 |
| R-free | 0.23585 |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.937 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.950 |
| High resolution limit [Å] | 2.877 | 2.900 |
| Rmerge | 0.091 | 0.800 |
| Number of reflections | 147557 | |
| <I/σ(I)> | 14.1 | |
| Completeness [%] | 94.6 | 84.9 |
| Redundancy | 3.8 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 25% PEG 3350 |
