5XOS
Crystal structure of HLA-B35 in complex with a pepetide antigen
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17B1 |
Synchrotron site | SSRF |
Beamline | BL17B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-08-01 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97916 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 50.702, 81.915, 110.084 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.726 - 1.697 |
R-factor | 0.14 |
Rwork | 0.138 |
R-free | 0.18380 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1a9e |
RMSD bond length | 0.003 |
RMSD bond angle | 0.784 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.5_2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.760 |
High resolution limit [Å] | 1.697 | 1.697 |
Rmerge | 0.077 | |
Number of reflections | 51567 | |
<I/σ(I)> | 25.433 | 5.981 |
Completeness [%] | 99.8 | 99.8 |
Redundancy | 7 | 6.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 288 | 0.1M MES monohydrate, pH 6.5, 12%(w/v) PEG20000 |