5Y91
The structure of the MHC class I molecule of bony fishes provides insights into the conserved nature of the antigen-presenting system
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U1 |
Synchrotron site | SSRF |
Beamline | BL17U1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-19 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97931 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 119.280, 50.413, 86.077 |
Unit cell angles | 90.00, 124.08, 90.00 |
Refinement procedure
Resolution | 32.883 - 1.901 |
R-factor | 0.1918 |
Rwork | 0.190 |
R-free | 0.22350 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2yez |
RMSD bond length | 0.003 |
RMSD bond angle | 0.765 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.5_2) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.900 |
Number of reflections | 31840 |
<I/σ(I)> | 17.711 |
Completeness [%] | 99.0 |
Redundancy | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291 | 0.2 M ammonium citrate tribasic, pH 7.0 and 20% w/v polyethylene glycol 3,350 |