5DYF
The crystal structure of Aminopeptidase N in complex with N-benzyl-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 | 2015-06-15 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9794 |
Spacegroup name | H 3 |
Unit cell lengths | 224.644, 224.644, 57.938 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 28.650 - 1.854 |
R-factor | 0.1474 |
Rwork | 0.146 |
R-free | 0.17440 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2gtq |
RMSD bond length | 0.005 |
RMSD bond angle | 0.915 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | MOLREP |
Refinement software | PHENIX (dev_1888) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 28.650 |
High resolution limit [Å] | 1.854 |
Rmerge | 0.070 |
Number of reflections | 119960 |
<I/σ(I)> | 18.7 |
Completeness [%] | 99.9 |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 291 | 2.0 M Ammonium Sulfate |