5U98
The crystal structure of a self-peptide complexed to Abacavir and HLA-B*57:01
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X6A |
Synchrotron site | NSLS |
Beamline | X6A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-08-30 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9436 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.134, 132.602, 87.964 |
Unit cell angles | 90.00, 104.99, 90.00 |
Refinement procedure
Resolution | 28.323 - 2.000 |
R-factor | 0.1739 |
Rwork | 0.173 |
R-free | 0.21650 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3upr |
RMSD bond length | 0.007 |
RMSD bond angle | 1.052 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 28.323 |
High resolution limit [Å] | 2.000 |
Rmerge | 0.270 |
Number of reflections | 69488 |
<I/σ(I)> | 30.398 |
Completeness [%] | 95.0 |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 289 | 0.1M NACACODYLATE, 0.1MNAACETATE, 25% PEG 8,000, 15% GLYCEROL |