4PGC
MHC Class I in complex with modified Sendai virus nucleoprotein peptide FAPGN(3,5-diiodotyrosine)PAL
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 | 2012-05-24 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.87260 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 66.179, 90.303, 89.370 |
Unit cell angles | 90.00, 111.58, 90.00 |
Refinement procedure
Resolution | 83.108 - 2.300 |
R-factor | 0.2135 |
Rwork | 0.212 |
R-free | 0.24280 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1rjz |
RMSD bond length | 0.006 |
RMSD bond angle | 1.171 |
Data scaling software | SCALA (3.3.16) |
Phasing software | PHASER |
Refinement software | REFMAC (refmac_5.8.0071) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 83.108 | 50.790 | 2.420 |
High resolution limit [Å] | 2.300 | 7.270 | 2.300 |
Rmerge | 0.029 | 0.529 | |
Rmeas | 0.091 | ||
Rpim | 0.048 | 0.018 | 0.329 |
Total number of observations | 152881 | 4718 | 22281 |
Number of reflections | 43356 | ||
<I/σ(I)> | 12 | 32.2 | 2.2 |
Completeness [%] | 99.5 | 98.3 | 99.4 |
Redundancy | 3.5 | 3.3 | 3.5 |
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) |