3O4I
Structure and Catalysis of Acylaminoacyl Peptidase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-07-29 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.9999 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 103.630, 209.890, 205.920 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.800 - 2.700 |
| R-factor | 0.20934 |
| Rwork | 0.207 |
| R-free | 0.25192 |
| 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 | 1.734 |
| 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 | 2.770 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.094 | 0.527 |
| Number of reflections | 61532 | |
| <I/σ(I)> | 13.2 | 3.3 |
| Completeness [%] | 99.3 | 99.8 |
| Redundancy | 5.94 | 6.26 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 293 | 78mM sodium acetate, 0.44mM EDTA, 6.7mM dithiothreitol, 2.0% PEG 4000 , pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
