2A83
Crystal structure of hla-b*2705 complexed with the glucagon receptor (gr) peptide (residues 412-420)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-04-05 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.933 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 50.982, 82.083, 65.316 |
Unit cell angles | 90.00, 108.73, 90.00 |
Refinement procedure
Resolution | 28.990 - 1.400 |
R-factor | 0.12734 |
Rwork | 0.126 |
R-free | 0.14955 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1jge |
RMSD bond length | 0.012 |
RMSD bond angle | 1.480 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | EPMR |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.420 |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.039 | 0.112 |
Number of reflections | 97993 | |
Completeness [%] | 97.9 | 87.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | 14% PEG4000,100mM Tris/HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |