4OV5
Structure of HLA-DR1 with a bound peptide with non-optimal alanine in the P1 pocket
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-03-09 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 95.955, 173.188, 96.484 |
| Unit cell angles | 90.00, 109.72, 90.00 |
Refinement procedure
| Resolution | 41.511 - 2.199 |
| R-factor | 0.2069 |
| Rwork | 0.205 |
| R-free | 0.23950 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1aqd |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.773 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.000 | 2.240 |
| High resolution limit [Å] | 2.199 | 2.199 |
| Rmerge | 0.048 | 0.477 |
| Number of reflections | 140577 | |
| <I/σ(I)> | 16.09 | 1.44 |
| Completeness [%] | 93.7 | 81.8 |
| Redundancy | 2.5 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 277 | 4% PEG4000, 10% ethylene glycol, 100 mM sodium acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
