6PMD
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 | 2012-11-30 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 94.377, 125.972, 145.603 |
| Unit cell angles | 90.00, 93.77, 90.00 |
Refinement procedure
| Resolution | 38.800 - 2.210 |
| R-factor | 0.2009 |
| Rwork | 0.200 |
| R-free | 0.22720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3sta |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.433 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0222) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.260 |
| High resolution limit [Å] | 2.210 | 6.020 | 2.220 |
| Rmerge | 0.134 | 0.063 | 0.552 |
| Rmeas | 0.150 | 0.070 | 0.636 |
| Rpim | 0.065 | 0.030 | 0.309 |
| Number of reflections | 166305 | 8500 | 7872 |
| <I/σ(I)> | 8.2 | ||
| Completeness [%] | 99.7 | 99.7 | 95.1 |
| Redundancy | 5.2 | 5.3 | 4 |
| CC(1/2) | 0.996 | 0.749 |
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, 0.02M CaCl2 |
