5NIG
Crystal structure of HLA-DRB1*04:01 with modified alpha-enolase peptide 326-340 (arginine 327 to citrulline)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-1 |
Synchrotron site | ESRF |
Beamline | MASSIF-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-05-13 |
Detector | DECTRIS PILATUS3 2M |
Wavelength(s) | 0.966 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 68.606, 128.319, 53.521 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.860 - 1.350 |
R-factor | 0.14281 |
Rwork | 0.142 |
R-free | 0.18080 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5ni9 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.550 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 46.860 |
High resolution limit [Å] | 1.350 |
Number of reflections | 103630 |
<I/σ(I)> | 9.9 |
Completeness [%] | 98.9 |
Redundancy | 4.4 |
CC(1/2) | 0.996 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 0.1 M MES pH 6.5 10% (vol/vol) MPD 15% (vol/vol) PEG 3350 |