5GRD
Crystal structure of 10-mer peptide from EBV in complex with HLA-A1101.
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 | 2015-09-25 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9999 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.422, 67.795, 115.295 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 58.440 - 1.800 |
R-factor | 0.17928 |
Rwork | 0.177 |
R-free | 0.22595 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1x7q |
RMSD bond length | 0.020 |
RMSD bond angle | 1.881 |
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] | 58.440 |
High resolution limit [Å] | 1.800 |
Number of reflections | 37049 |
<I/σ(I)> | 6.85 |
Completeness [%] | 96.7 |
Redundancy | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 290 | 0.2 M ammonium acetate, 0.1 M Sodium acetate trihydrate, 30% PEG4000 |