3QXD
F54C HLA-DR1 bound with CLIP peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-19 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.08 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 65.001, 94.870, 154.090 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.185 - 2.302 |
| R-factor | 0.1901 |
| Rwork | 0.189 |
| R-free | 0.22100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sje |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.818 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.1.4) |
| Refinement software | PHENIX (1.7_650) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 6.240 | 2.300 |
| Rmerge | 0.069 | 0.026 | 0.410 |
| Number of reflections | 43039 | ||
| <I/σ(I)> | 10.2 | ||
| Completeness [%] | 100.0 | 99.4 | 100 |
| Redundancy | 7.4 | 6.8 | 7.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 277 | PEG 4000, 10% Glycerol, 100mM Sodium Acetate pH 5.6, 5mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
