3BP7
The high resolution crystal structure of HLA-B*2709 in complex with a Cathepsin A signal sequence peptide, pCatA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-01-18 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.95373 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.195, 83.002, 110.779 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.080 - 1.800 |
| R-factor | 0.169 |
| Rwork | 0.167 |
| R-free | 0.20400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jge |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.631 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.850 |
| High resolution limit [Å] | 1.790 | 1.790 |
| Rmerge | 0.057 | 0.331 |
| Number of reflections | 41600 | |
| <I/σ(I)> | 19.4 | 3.07 |
| Completeness [%] | 93.3 | 84.3 |
| Redundancy | 3.6 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | 23.5% PEG 8000, 0.1M Tris buffer pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
