4S2R
Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: a cytosolic enzyme with a di-nuclear active site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04-1 |
| Synchrotron site | Diamond |
| Beamline | I04-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-01-29 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.917 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 141.377, 87.910, 114.764 |
| Unit cell angles | 90.00, 115.92, 90.00 |
Refinement procedure
| Resolution | 38.872 - 1.949 |
| R-factor | 0.1658 |
| Rwork | 0.163 |
| R-free | 0.21410 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ctz |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.028 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.872 | 1.980 |
| High resolution limit [Å] | 1.930 | 1.930 |
| Rmerge | 0.049 | 0.441 |
| Number of reflections | 91904 | |
| <I/σ(I)> | 14.9 | 1.9 |
| Completeness [%] | 97.2 | 82.7 |
| Redundancy | 3.7 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 0.2 M sodium malonate, 0.1 M Bis-Tris propane, pH 8.5, 17.5% w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP |
