5ENW
Structure of HLA-A2:01 with peptide G9L
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 12.3.1 |
Synchrotron site | ALS |
Beamline | 12.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-09-17 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.474, 80.483, 57.075 |
Unit cell angles | 90.00, 113.41, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.850 |
R-factor | 0.21007 |
Rwork | 0.208 |
R-free | 0.24354 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3mre |
RMSD bond length | 0.006 |
RMSD bond angle | 1.129 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0124) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.890 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.128 | 0.575 |
Number of reflections | 35425 | |
<I/σ(I)> | 21.5 | 3.1 |
Completeness [%] | 93.2 | 96.1 |
Redundancy | 2.7 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 30% PEG 4000, 0.1M Tris-HCl pH 8.0, 0.2M lithium sulfate |