5DZK
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 | 2014-06-06 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 205.940, 183.350, 188.450 |
| Unit cell angles | 90.00, 94.44, 90.00 |
Refinement procedure
| Resolution | 72.240 - 3.070 |
| R-factor | 0.19989 |
| Rwork | 0.198 |
| R-free | 0.23167 |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.944 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 3.150 |
| High resolution limit [Å] | 3.070 | 3.070 |
| Rmerge | 0.105 | 0.666 |
| Number of reflections | 129368 | |
| <I/σ(I)> | 11.33 | 2.29 |
| Completeness [%] | 99.5 | |
| Redundancy | 4.22 | 4.29 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 25% PEG 3350 |
