4QPE
Crystal structure of Aminopeptidase N in complex with N-cyclohexyl-1,2-diaminoethylphosphonic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-09-10 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9794 |
| Spacegroup name | H 3 |
| Unit cell lengths | 224.495, 224.495, 57.951 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.062 - 2.004 |
| R-factor | 0.1724 |
| Rwork | 0.171 |
| R-free | 0.20170 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gtq |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.698 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: dev_1639)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.062 | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.100 | |
| Number of reflections | 71931 | |
| <I/σ(I)> | 11.3 | |
| Completeness [%] | 98.3 | 94 |
| Redundancy | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 2.0 M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
