3PGC
Crystal Structure of HLA-DR1 with CLIP106-120, flipped peptide orientation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.1 |
Synchrotron site | BESSY |
Beamline | 14.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-11-03 |
Detector | Rayonix |
Wavelength(s) | 0.91841 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 138.146, 138.146, 104.520 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 34.537 - 2.660 |
R-factor | 0.2009 |
Rwork | 0.198 |
R-free | 0.25010 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.132 |
Data scaling software | XSCALE |
Phasing software | PHASER (2.1.4) |
Refinement software | PHENIX (1.5_2) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 34.537 | 34.537 | 2.730 |
High resolution limit [Å] | 2.660 | 11.900 | 2.660 |
Rmerge | 0.081 | 0.025 | 0.679 |
Number of reflections | 33394 | 397 | 2417 |
<I/σ(I)> | 17.96 | 42.8 | 3 |
Completeness [%] | 99.9 | 93.4 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 298 | PEG 1500, MIB buffer, pH 6.0, vapor diffusion, sitting drop, temperature 298K |