3BO8
The High Resolution Crystal Structure of HLA-A1 Complexed with the MAGE-A1 Peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-05-20 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.954 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.176, 74.060, 125.940 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.650 - 1.800 |
| R-factor | 0.196 |
| Rwork | 0.195 |
| R-free | 0.22500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1w72 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.451 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 63.888 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.109 | 0.351 |
| Total number of observations | 24361 | |
| Number of reflections | 43828 | |
| <I/σ(I)> | 17.3 | 3.82 |
| Completeness [%] | 97.0 | 95 |
| Redundancy | 4.1 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 20% PEG 3350, 0.2M Sodium Fluoride, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
