3O4G
Structure and Catalysis of Acylaminoacyl Peptidase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X12 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X12 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-12-15 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9786 |
| Spacegroup name | P 1 |
| Unit cell lengths | 71.212, 97.016, 109.494 |
| Unit cell angles | 89.01, 109.20, 100.21 |
Refinement procedure
| Resolution | 19.640 - 2.500 |
| R-factor | 0.21755 |
| Rwork | 0.215 |
| R-free | 0.26166 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Hydrolase and propeller domains of PDB entry 2HU5. |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.218 |
| 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] | 20.000 | 2.560 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.089 | 0.595 |
| Number of reflections | 88675 | |
| <I/σ(I)> | 12.55 | 2.01 |
| Completeness [%] | 94.1 | 94.9 |
| Redundancy | 1.99 | 1.99 |
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 |
