5FA3
Structure of HLA-A2:01 with peptide G9V
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-07-22 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.12 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 56.201, 79.259, 57.397 |
| Unit cell angles | 90.00, 115.98, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.860 |
| R-factor | 0.21116 |
| Rwork | 0.210 |
| R-free | 0.23491 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5mre |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.109 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0124) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.890 |
| High resolution limit [Å] | 1.860 | 1.860 |
| Rmerge | 0.311 | |
| Number of reflections | 37513 | |
| <I/σ(I)> | 20.3 | 4.6 |
| Completeness [%] | 98.8 | 97.5 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 30% PEG 4000, 0.1M Tris-HCl pH 8.0, 0.2 M lithium sulfate |
