1CE6
MHC CLASS I H-2DB COMPLEXED WITH A SENDAI VIRUS NUCLEOPROTEIN PEPTIDE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX7.2 |
| Synchrotron site | SRS |
| Beamline | PX7.2 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 60.787, 58.082, 74.666 |
| Unit cell angles | 90.00, 108.26, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.900 |
| R-factor | 0.217 * |
| Rwork | 0.217 |
| R-free | 0.27400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 1HOC AND 3HLA |
| RMSD bond length | 0.008 |
| RMSD bond angle | 24.700 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (0.4) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.920 |
| High resolution limit [Å] | 2.850 | 2.850 |
| Rmerge | 0.096 * | 0.376 * |
| Number of reflections | 11481 | |
| <I/σ(I)> | 10 | 2.6 |
| Completeness [%] | 96.1 | 86.2 |
| Redundancy | 2.6 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.5 * | 4 * | pH 5.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | peptide complex | 10 (mg/ml) | |
| 2 | 1 | drop | Tris buffered saline | ||
| 3 | 1 | reservoir | PEG6000 | 15-23 (%) | |
| 4 | 1 | reservoir | ammonium sulfate | 100 (mM) | |
| 5 | 1 | reservoir | MES | 100 (mM) |
