4NO2
Crystal structure of RQA_V phosphopeptide bound to HLA-A2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-03-15 |
| Detector | RIGAKU SATURN 944 |
| Wavelength(s) | 1.5417 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 119.200, 54.700, 75.200 |
| Unit cell angles | 90.00, 104.80, 90.00 |
Refinement procedure
| Resolution | 19.865 - 2.000 |
| R-factor | 0.2098 |
| Rwork | 0.208 |
| R-free | 0.24870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3bh9 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.171 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 19.865 | 19.865 | 2.100 |
| High resolution limit [Å] | 2.000 | 10.000 | 2.000 |
| Rmerge | 0.053 | 0.020 | 0.465 |
| Number of reflections | 31595 | 243 | 4172 |
| <I/σ(I)> | 32.54 | 114.75 | 4.35 |
| Completeness [%] | 98.9 | 85.3 | 96.1 |
| Redundancy | 10 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 20% PEG8000, 0.1 M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
