1W0W
Crystal Structure Of HLA-B*2709 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 | 51.175, 82.670, 110.177 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 65.940 - 2.110 |
| R-factor | 0.186 |
| Rwork | 0.182 |
| R-free | 0.24500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1w0v |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.238 |
| 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] | 28.100 | 2.180 |
| High resolution limit [Å] | 2.110 | 2.110 |
| Rmerge | 0.103 | 0.320 |
| Number of reflections | 22935 | |
| <I/σ(I)> | 10 | 2 |
| Completeness [%] | 87.0 | 86 |
| Redundancy | 2.6 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 20% PEG8000, 0.1M TRIS PH 8.5 |
