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 |