4S2T
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 I24 |
| Synchrotron site | Diamond |
| Beamline | I24 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-08-13 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.968 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 140.590, 86.810, 113.130 |
| Unit cell angles | 90.00, 115.96, 90.00 |
Refinement procedure
| Resolution | 38.520 - 2.150 |
| R-factor | 0.20668 |
| Rwork | 0.205 |
| R-free | 0.24740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | native C. elegans APP-1 structure |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.227 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.520 | 2.210 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.063 | 0.453 |
| Number of reflections | 61133 | |
| <I/σ(I)> | 13.3 | 2.4 |
| Completeness [%] | 91.8 | 60.4 |
| Redundancy | 2.6 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 0.2 M sodium iodide, 0.1 M Bis-Tris propane, pH 7.5, 20 % w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP |
