3FES
Crystal Structure of the ATP-dependent Clp Protease ClpC from Clostridium difficile
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-11-26 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 |
| Unit cell lengths | 34.690, 68.523, 81.339 |
| Unit cell angles | 66.91, 86.23, 85.33 |
Refinement procedure
| Resolution | 34.550 - 1.820 |
| R-factor | 0.189 |
| Rwork | 0.187 |
| R-free | 0.22200 |
| Structure solution method | SAD |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.517 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.5.0053) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.550 | 1.850 |
| High resolution limit [Å] | 1.820 | 1.820 |
| Rmerge | 0.069 | 0.482 |
| Number of reflections | 59636 | |
| <I/σ(I)> | 14.1 | 1.9 |
| Completeness [%] | 96.6 | 95.6 |
| Redundancy | 2.6 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 297 | 0.2 M MgCl2, 0.1 M Citrate pH 5.5, 40% (v/v) PEG-400, VAPOR DIFFUSION, HANGING DROP, temperature 297K |
