3O4J
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 | 2009-12-12 |
| Detector | MAR555 FLAT PANEL |
| Wavelength(s) | 0.8148 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 184.270, 227.524, 110.684 |
| Unit cell angles | 90.00, 100.37, 90.00 |
Refinement procedure
| Resolution | 29.520 - 2.500 |
| R-factor | 0.20099 |
| Rwork | 0.199 |
| R-free | 0.23589 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Hydrolase and propeller domains of PDB entry 2HU5. |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.748 |
| 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 | 2.600 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.092 | 0.642 |
| Number of reflections | 149375 | |
| <I/σ(I)> | 11.43 | 2.48 |
| Completeness [%] | 96.8 | 98.8 |
| Redundancy | 3.3 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 170mM sodium acetate, 0.4mM EDTA, 10% dimethyl sulphoxide, 2.5% PEG 4000 , pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
