4DYO
Crystal Structure of Human Aspartyl Aminopeptidase (DNPEP) in complex with Aspartic acid Hydroxamate
Replaces: 3L6SExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-11-25 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9763 |
| Spacegroup name | F 4 3 2 |
| Unit cell lengths | 244.595, 244.595, 244.595 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 54.690 - 2.200 |
| R-factor | 0.156 |
| Rwork | 0.155 |
| R-free | 0.19470 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ijz |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.522 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0089) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.110 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.179 | 0.833 |
| Number of reflections | 32185 | |
| <I/σ(I)> | 10.4 | 2.2 |
| Completeness [%] | 99.6 | 97.5 |
| Redundancy | 10.8 | 8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293.15 | 15% PEG3350, 0.25 M magnesium chloride, 0.1 M Tris, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K |
