5GRG
Crystal structure of dual peptide from EBV in complex with HLA-A*11:01
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-07-10 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9999 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 55.246, 67.432, 115.017 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 58.170 - 1.940 |
| R-factor | 0.19177 |
| Rwork | 0.189 |
| R-free | 0.24295 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1x7q |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.777 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 58.170 |
| High resolution limit [Å] | 1.940 |
| Number of reflections | 30594 |
| <I/σ(I)> | 2.5 |
| Completeness [%] | 99.5 |
| Redundancy | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 290 | 0.1 M Ammonium acetate, 0.1 M Bis-Tris, 22% PEG 4000 |
