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 |