3VFM
crystal structure of HLA B*3508 LPEP155A, HLA mutant Ala155
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 | 2011-04-08 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.9536 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.384, 81.909, 112.256 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.237 - 1.900 |
| R-factor | 0.1931 |
| Rwork | 0.191 |
| R-free | 0.24060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1zhk |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.019 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.7.1_743) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 100.000 |
| High resolution limit [Å] | 1.900 |
| Number of reflections | 37187 |
| Completeness [%] | 99.4 |
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 |






