3CZF
Crystal structure of HLA-B*2709 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 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 50.946, 81.933, 65.397 |
Unit cell angles | 90.00, 108.91, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.200 |
R-factor | 0.13 |
Rwork | 0.129 |
R-free | 0.14900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1k5n |
RMSD bond length | 0.011 |
RMSD bond angle | 1.427 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | EPMR |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.120 |
High resolution limit [Å] | 1.100 | 1.100 |
Number of reflections | 196702 | |
<I/σ(I)> | 20.8 | 2.7 |
Completeness [%] | 95.8 | 90.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 291 | 14% (w/v) PEG 4000, 20mM Tris/HCl pH 7.5, 150mM NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 291K, pH 7.50 |