5IB1
Crystal structure of HLA-B*27:05 complexed with the self-peptide pVIPR measured at 295 K
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 295 |
| Detector technology | CCD |
| Collection date | 2011-05-26 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.9184 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.533, 83.111, 66.543 |
| Unit cell angles | 90.00, 109.35, 90.00 |
Refinement procedure
| Resolution | 29.367 - 1.910 |
| R-factor | 0.1653 |
| Rwork | 0.164 |
| R-free | 0.19150 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1of2 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.907 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10_2155: 000)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.960 |
| High resolution limit [Å] | 1.910 | 1.910 |
| Number of reflections | 40810 | |
| <I/σ(I)> | 12.92 | 1.7 |
| Completeness [%] | 99.2 | 93.4 |
| Redundancy | 3.3 | 2.8 |
| CC(1/2) | 0.998 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | 0.1 M Tris HCl, 16% (w/v) PEG 8000 |
