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 |