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) |
