3PWN
Human Class I MHC HLA-A2 in complex with the HuD (G2L) peptide variant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-04-15 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 58.242, 84.433, 83.908 |
| Unit cell angles | 90.00, 89.98, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.600 |
| R-factor | 0.1812 |
| Rwork | 0.179 |
| R-free | 0.21440 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1duz |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.670 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 20.000 | 20.000 | 1.630 |
| High resolution limit [Å] | 1.600 | 4.330 | 1.600 |
| Rmerge | 0.075 | 0.034 | 0.507 |
| Number of reflections | 102975 | ||
| <I/σ(I)> | 18.8 | ||
| Completeness [%] | 96.1 | 99.1 | 85.9 |
| Redundancy | 3.6 | 3.7 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | PEG3350 24%, MES 0.025M, NaCl 0.1M, pH 6.5, vapor diffusion, sitting drop, temperature 277K |
