6X00
Structure of DbNA(11) peptides bound to H-2Db MHC-I
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-05-02 |
Detector | ADSC QUANTUM 210r |
Wavelength(s) | 0.954 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 69.010, 44.751, 71.657 |
Unit cell angles | 90.00, 98.45, 90.00 |
Refinement procedure
Resolution | 45.910 - 1.550 |
R-factor | 0.186 |
Rwork | 0.184 |
R-free | 0.21500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ftg |
RMSD bond length | 0.010 |
RMSD bond angle | 0.980 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | BUSTER |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.910 | 1.580 |
High resolution limit [Å] | 1.550 | 1.550 |
Rpim | 0.056 | 0.439 |
Number of reflections | 62822 | 3067 |
<I/σ(I)> | 12.7 | 2 |
Completeness [%] | 99.5 | |
Redundancy | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.7 | 298 | 0.1M sodium citrate pH 5.7, 0.2M Li2SO4 and 24-28% (w/v) PEG3350 |