1JGE
HLA-B*2705 bound to nona-peptide m9
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID13 |
Synchrotron site | ESRF |
Beamline | ID13 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-07-10 |
Detector | MARRESEARCH |
Wavelength(s) | 0.964 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.300, 83.200, 110.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.700 * - 2.100 |
R-factor | 0.1945 |
Rwork | 0.192 |
R-free | 0.25000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1hsa |
RMSD bond length | 0.014 |
RMSD bond angle | 1.400 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.700 | 2.110 |
High resolution limit [Å] | 2.070 | 2.070 |
Rmerge | 0.049 | 0.179 * |
Number of reflections | 26964 * | 1931 * |
<I/σ(I)> | 30.7 | 6.5 |
Completeness [%] | 91.3 * | 67.1 * |
Redundancy | 6 | 3.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 291 | used streak-seeding * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | drop | Tris | 20 (mM) | pH7.5 |
3 | 1 | drop | 150 (mM) | ||
4 | 1 | reservoir | PEG8000 | 28 (%) | |
5 | 1 | reservoir | Tris | 100 (mM) | pH8.0 |