3VFT
crystal structure of HLA B*3508LPEP-P6Ala, peptide mutant P6-ala
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-18 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.9536 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.700, 81.500, 111.300 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.773 - 1.947 |
| R-factor | 0.1744 |
| Rwork | 0.172 |
| R-free | 0.22320 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1zhk |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.073 |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.7.1_743) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 65.756 | 2.050 |
| High resolution limit [Å] | 1.947 | 1.950 |
| Rmerge | 0.141 | 0.454 |
| Number of reflections | 34385 | 4702 |
| <I/σ(I)> | 17.17 | 6.17 |
| Completeness [%] | 99.8 | 100 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | 0.2M ammonium acetate, 16% PEG 4K, 0.1M sodium citrate pH5.6, vapor diffusion, hanging drop, temperature 293K |
