6BIX
HLA-DRB1 in complex with citrullinated LL37 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-07-23 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.9537 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 67.337, 183.059, 78.435 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.528 - 2.200 |
| R-factor | 0.1709 |
| Rwork | 0.169 |
| R-free | 0.21250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4mdi |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.908 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.2.7) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 49.210 | 49.210 | 2.270 |
| High resolution limit [Å] | 2.200 | 9.070 | 2.200 |
| Rmerge | 0.117 | 0.047 | 0.332 |
| Rmeas | 0.130 | 0.053 | 0.369 |
| Rpim | 0.056 | 0.023 | 0.158 |
| Total number of observations | 2025 | 11890 | |
| Number of reflections | 25088 | 417 | 2137 |
| <I/σ(I)> | 8.3 | 13.3 | 4.2 |
| Completeness [%] | 100.0 | 99.6 | 100 |
| Redundancy | 5.5 | 4.9 | 5.6 |
| CC(1/2) | 0.991 | 0.993 | 0.895 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.3 | 294 | 22-28% PEG 3350, 0.2M Potassium Nitrate, 0.1M Bis-Tris-Propane pH 7.3 |
