3O4H
Structure and Catalysis of Acylaminoacyl Peptidase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2009-12-11 |
| Detector | MAR555 FLAT PANEL |
| Wavelength(s) | 0.8148 |
| Spacegroup name | P 1 |
| Unit cell lengths | 71.405, 97.979, 98.797 |
| Unit cell angles | 105.69, 103.52, 100.36 |
Refinement procedure
| Resolution | 24.620 - 1.820 |
| R-factor | 0.20468 |
| Rwork | 0.203 |
| R-free | 0.23366 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Hydrolase and propeller domains of PDB entry 2HU5. |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.722 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.870 |
| High resolution limit [Å] | 1.820 | 1.820 |
| Rmerge | 0.028 | 0.606 |
| Number of reflections | 206854 | |
| <I/σ(I)> | 22.72 | 2.26 |
| Completeness [%] | 95.2 | 94.1 |
| Redundancy | 1.88 | 1.88 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 78mM sodium acetate, 0.44mM EDTA, 6.7mM DITHIOTHREITOL, 2.4% PEG 4000 , pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
