5FA4
Structure of HLA-A2:01 with peptide Y16R
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-07-22 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.12 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 56.525, 79.421, 58.513 |
Unit cell angles | 90.00, 116.42, 90.00 |
Refinement procedure
Resolution | 48.860 - 2.400 |
R-factor | 0.20728 |
Rwork | 0.204 |
R-free | 0.25851 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3mre |
RMSD bond length | 0.009 |
RMSD bond angle | 1.335 |
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 | 2.440 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.542 | |
Number of reflections | 17776 | |
<I/σ(I)> | 11.3 | 1.7 |
Completeness [%] | 97.9 | 85.2 |
Redundancy | 3.4 | 3 |
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, 0.1M lithium sulfate |