5LDS
Structure of the porcine aminopeptidase N ectodomain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-06-12 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.8726 |
| Spacegroup name | P 1 |
| Unit cell lengths | 78.670, 78.770, 223.870 |
| Unit cell angles | 99.66, 92.62, 111.33 |
Refinement procedure
| Resolution | 24.961 - 2.000 |
| R-factor | 0.1713 |
| Rwork | 0.169 |
| R-free | 0.20650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.903 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 25.000 |
| High resolution limit [Å] | 2.000 |
| Rmerge | 0.087 |
| Number of reflections | 322701 |
| <I/σ(I)> | 8.5 |
| Completeness [%] | 97.5 |
| Redundancy | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 294 | 20% PEG-3350 and 100 mM sodium acetate pH 5.6 |
