4QUO
Crystal structure of Aminopeptidase N in complex with the phosphinic dipeptide analogue LL-(R,S)-hPheP[CH2]Phe(3-CH2NH2)
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 | 2013-10-20 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9794 |
| Spacegroup name | H 3 |
| Unit cell lengths | 223.707, 223.707, 57.769 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 27.980 - 1.650 |
| R-factor | 0.14983 |
| Rwork | 0.148 |
| R-free | 0.18188 |
| Structure solution method | SAD |
| Starting model (for MR) | 2gtq |
| RMSD bond length | 0.020 |
| RMSD bond angle | 2.035 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.680 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.070 | |
| Number of reflections | 129700 | |
| <I/σ(I)> | 18 | |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 291 | 2.0 M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
