4PG9
MHC Class I in complex with Sendai virus nucleoprotein peptide FAPGNYPAL
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-07-02 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.87260 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 87.721, 136.533, 45.203 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.400 |
R-factor | 0.2124 |
Rwork | 0.210 |
R-free | 0.24990 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3p9l |
RMSD bond length | 0.005 |
RMSD bond angle | 1.010 |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0030) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.530 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.127 | 0.488 |
Number of reflections | 21454 | |
<I/σ(I)> | 8.3 | 2.6 |
Completeness [%] | 98.3 | 98.9 |
Redundancy | 3.8 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | sodium/potassium phosphate buffer 1.9M, MPD 1%, glycerol (cryoprotection) |