6NCA
HLA-A2 (A*02:01) bound to a peptide from the Epstein-Barr virus BRLF1 protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-08-20 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 189.910, 100.170, 292.410 |
| Unit cell angles | 90.00, 94.43, 90.00 |
Refinement procedure
| Resolution | 111.419 - 3.300 |
| R-factor | 0.285442550216 |
| Rwork | 0.285 |
| R-free | 0.30270 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.779 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 111.420 | 3.050 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Number of reflections | 217116 | 10543 |
| <I/σ(I)> | 2.5 | |
| Completeness [%] | 98.7 | 97.3 |
| Redundancy | 3.3 | 3.3 |
| CC(1/2) | 0.915 | 0.161 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 277 | 10.5% (w/v) PEG 4000, 35 mM Tris base/ HCl (pH 8.5), 70 mM Li2SO4 |
