2RFX
Crystal Structure of HLA-B*5701, presenting the self peptide, LSSPVTKSF
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-11-08 |
| Detector | ADSC QUANTUM 210 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 64.844, 49.029, 70.666 |
| Unit cell angles | 90.00, 100.70, 90.00 |
Refinement procedure
| Resolution | 27.480 - 2.500 |
| R-factor | 0.21239 |
| Rwork | 0.209 |
| R-free | 0.26845 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2h6p |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.026 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 60.000 | 2.600 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.081 | 0.312 |
| Number of reflections | 15096 | |
| <I/σ(I)> | 18.8 | 5.1 |
| Completeness [%] | 94.3 | 89.8 |
| Redundancy | 3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
