1W0V
Crystal Structure Of HLA-B*2705 Complexed With the self-Peptide TIS from EGF-response factor 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2002-09-12 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.861, 82.488, 109.421 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 65.940 - 2.270 |
| R-factor | 0.187 |
| Rwork | 0.184 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jge |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.380 |
| Data reduction software | HKL |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.19) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.600 | 2.350 |
| High resolution limit [Å] | 2.270 | 2.270 |
| Rmerge | 0.090 | 0.230 |
| Number of reflections | 20780 | |
| <I/σ(I)> | 13 | 2.1 |
| Completeness [%] | 95.0 | 88.4 |
| Redundancy | 3.2 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 18% PEG8000, 0.1M TRIS PH 8.0 |
