3VFS
crystal structure of HLA B*3508LPEP-P5Ala , peptide mutant P5-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 | 50.771, 81.535, 111.450 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.799 - 1.850 |
R-factor | 0.173 |
Rwork | 0.171 |
R-free | 0.21610 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1zhk |
RMSD bond length | 0.007 |
RMSD bond angle | 1.080 |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.7.1_743) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 65.805 | 1.950 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.120 | 0.463 |
Number of reflections | 40200 | 5788 |
<I/σ(I)> | 15.1 | 5.07 |
Completeness [%] | 99.8 | 99.8 |
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 |