3FT3
Crystal Structure of the minor histocompatibility peptide HA-1His in complex with HLA-A2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-12-08 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.99 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 51.470, 79.750, 54.210 |
Unit cell angles | 90.00, 111.02, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.950 |
R-factor | 0.18406 |
Rwork | 0.182 |
R-free | 0.23054 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.119 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.020 |
High resolution limit [Å] | 1.950 | 1.950 |
Number of reflections | 29304 | |
<I/σ(I)> | 10.1 | 3.4 |
Completeness [%] | 97.9 | 94.8 |
Redundancy | 4.1 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 12-15% w/v PEG 6000, 0.1 M NaCl and 0.1 M tri-sodium-citrate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |