5VZ2
Structure of ClpP from Staphylococcus aureus in complex with Acyldepsipeptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-BM |
| Synchrotron site | APS |
| Beamline | 22-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-06-13 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 94.562, 126.131, 145.794 |
| Unit cell angles | 90.00, 93.42, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.260 |
| R-factor | 0.1796 |
| Rwork | 0.179 |
| R-free | 0.21870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3sta |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.823 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.350 |
| High resolution limit [Å] | 2.270 | 4.890 | 2.270 |
| Rmerge | 0.067 | 0.039 | 0.302 |
| Total number of observations | 614075 | ||
| Number of reflections | 155067 | ||
| <I/σ(I)> | 10.8 | ||
| Completeness [%] | 97.3 | 99.8 | 90.4 |
| Redundancy | 4 | 4.6 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 291.15 | 0.1 M NaOAc pH 4.5, 18-35% MPD, and 0.02 M CaCl2 |
