3LN4
Crystal structure of HLA-B*4103 in complex with a 16mer self-peptide derived from heterogeneous nuclear ribonucleoproteins C1/C2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-12-13 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.777, 81.992, 109.810 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.918 - 1.296 |
| R-factor | 0.1549 |
| Rwork | 0.155 |
| R-free | 0.17660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1syv |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.101 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 65.600 | 1.350 |
| High resolution limit [Å] | 1.296 | 1.296 |
| Rmerge | 0.066 | 0.364 |
| Number of reflections | 110817 | |
| <I/σ(I)> | 16.8 | 4.2 |
| Completeness [%] | 97.2 | 88.6 |
| Redundancy | 7.4 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 294 | 0.1M citrate pH 5.6, 14-20% PEG 4000, 0.2M NH4OAc, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
