6O9B
Crystal structure of HLA-A3*01 in complex with a wild-type beta-catenin peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS-II BEAMLINE 17-ID-2 |
| Synchrotron site | NSLS-II |
| Beamline | 17-ID-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-06-23 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 6 2 2 |
| Unit cell lengths | 152.770, 152.770, 84.835 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.870 - 2.200 |
| R-factor | 0.1846 |
| Rwork | 0.182 |
| R-free | 0.22680 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2xpg |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.932 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.21) |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 28.870 | 28.870 | 2.260 |
| High resolution limit [Å] | 2.200 | 9.060 | 2.200 |
| Rmerge | 0.164 | 0.052 | 1.081 |
| Rmeas | 0.172 | 0.055 | 1.138 |
| Rpim | 0.052 | 0.017 | 0.348 |
| Total number of observations | 313372 | ||
| Number of reflections | 29999 | 501 | 2345 |
| <I/σ(I)> | 9.7 | ||
| Completeness [%] | 99.2 | 96.7 | 91.2 |
| Redundancy | 10.4 | 9.3 | 9.8 |
| CC(1/2) | 0.996 | 0.998 | 0.704 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 292 | 0.1 M MES/imidazole, pH 6.5, 0.03 M diethylene glycol, 0.03 M triethylene glycol, 0.03 M tetraethylene glycol, 0.03 M pentaethylene glycol, 20% PEG500 MME, 10% PEG20000 |
