3SPV
Crystal structure of a peptide-HLA complex
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 | 2010-11-18 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.984 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.560, 81.460, 110.020 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.584 - 1.300 |
| R-factor | 0.1971 |
| Rwork | 0.196 |
| R-free | 0.21920 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1m05 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.036 |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.6.1_357) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 100.000 | 1.400 | |
| High resolution limit [Å] | 1.300 | 10.000 | 1.300 |
| Rmerge | 0.074 | 0.033 | 0.454 |
| Rmeas | 0.036 | 0.485 | |
| Number of reflections | 111282 | 240 | 21688 |
| <I/σ(I)> | 14.9 | 30.48 | 4.36 |
| Completeness [%] | 99.1 | 79.7 | 98.1 |
| Redundancy | 8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 5.6 | 298 | 15-20% PEG 4000, 0.2M ammonium acetate, 0.1M Na-Citrate, pH 5.6, vapor diffusion, temperature 298K |
