3MDJ
ER Aminopeptidase, ERAP1, Bound to the Zinc Aminopeptidase Inhibitor, Bestatin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Detector technology | CCD |
| Collection date | 2008-06-21 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0809 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 71.029, 234.635, 95.860 |
| Unit cell angles | 90.00, 103.59, 90.00 |
Refinement procedure
| Resolution | 38.106 - 2.950 |
| R-factor | 0.202 |
| Rwork | 0.199 |
| R-free | 0.26420 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1z5h |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.850 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.5_2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 3.060 |
| High resolution limit [Å] | 2.950 | 2.950 |
| Rmerge | 0.162 | |
| Number of reflections | 63768 | |
| <I/σ(I)> | 5.1 | 1.1 |
| Completeness [%] | 99.8 | 98.8 |
| Redundancy | 3.6 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 14% PEG 8000, 0.1M Bicine pH 8.5, 1mM Glutathione, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
