1MUJ
Crystal structure of murine class II MHC I-Ab in complex with a human CLIP peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL11-1 |
Synchrotron site | SSRL |
Beamline | BL11-1 |
Temperature [K] | 95 |
Detector technology | IMAGE PLATE |
Collection date | 2001-02-17 |
Detector | MAR scanner 300 mm plate |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 63.647, 88.065, 83.740 |
Unit cell angles | 90.00, 92.48, 90.00 |
Refinement procedure
Resolution | 33.060 - 2.150 |
R-factor | 0.22 |
Rwork | 0.220 |
R-free | 0.25000 * |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 26.400 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 33.060 | 2.230 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.038 * | 0.540 * |
Number of reflections | 24657 | |
<I/σ(I)> | 24.1 | 1.65 |
Completeness [%] | 98.0 | 97 |
Redundancy | 1.87 | 1.83 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 22 * | PEG3000, Sodium Chloride, Tris, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295.5K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | Tris | 100 (mM) | pH7.5 |
2 | 1 | reservoir | 200 (mM) | ||
3 | 1 | reservoir | PEG3000 | 22.5 (%) | |
4 | 1 | reservoir | MPD | 5 (%(v/v)) | |
5 | 1 | drop | protein | 5-10 (mg/ml) |