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 |