6VPZ
HLA-B*27:05 presenting an HIV-1 11mer peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 105 |
Detector technology | CCD |
Collection date | 2010-07-17 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.8726 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.250, 83.070, 110.120 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 66.320 - 2.100 |
R-factor | 0.1926 |
Rwork | 0.190 |
R-free | 0.23490 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1w0v |
RMSD bond length | 0.014 |
RMSD bond angle | 1.230 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.22) |
Phasing software | PHASER (2.6.1) |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 66.320 | 66.320 | 2.210 |
High resolution limit [Å] | 2.100 | 6.640 | 2.100 |
Rmerge | 0.054 | 0.803 | |
Rmeas | 0.222 | 0.060 | 0.866 |
Rpim | 0.083 | 0.024 | 0.322 |
Number of reflections | 28236 | 1013 | 4054 |
<I/σ(I)> | 8.4 | 6.5 | 0.9 |
Completeness [%] | 100.0 | 99.9 | 100 |
Redundancy | 7.1 | 6.4 | 7.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.3 | 277 | 20 %w/v Polyethylene Glycol 3350, 0.2 M Ammonium Chloride |