5DDH
Structure of HLA-A2:01 with the 12-mer peptide F12K
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) | 1.1 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 54.075, 79.769, 57.561 |
Unit cell angles | 90.00, 115.13, 90.00 |
Refinement procedure
Resolution | 29.900 - 1.500 |
R-factor | 0.198 |
Rwork | 0.198 |
R-free | 0.21800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3mre |
RMSD bond length | 0.006 |
RMSD bond angle | 1.091 |
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] | 40.000 | 1.530 |
High resolution limit [Å] | 1.500 | 1.500 |
Number of reflections | 70232 | |
<I/σ(I)> | 34.11 | 2.7 |
Completeness [%] | 99.4 | 99.7 |
Redundancy | 3.3 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293.15 | 30% PEG 4000, 0.1M Tris-HCl 8.0, 0.2M lithium sulfate |