3MRE
Crystal Structure of MHC class I HLA-A2 molecule complexed with EBV bmlf1-280-288 nonapeptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-12-16 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.93100 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.550, 79.430, 55.580 |
| Unit cell angles | 90.00, 112.29, 90.00 |
Refinement procedure
| Resolution | 15.000 - 1.100 |
| R-factor | 0.181 |
| Rwork | 0.181 |
| R-free | 0.20400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gso |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.213 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.5.0044) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.130 | |
| High resolution limit [Å] | 1.100 | 4.920 | 1.100 |
| Rmerge | 0.090 | 0.039 | 0.399 |
| Number of reflections | 150866 | 1924 | 10414 |
| <I/σ(I)> | 9.9 | 37 | 2.2 |
| Completeness [%] | 90.0 | 98.4 | 80.3 |
| Redundancy | 3.72 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 15% PEG 6000, 0.1M NaCitrate, 0.1M NaCl, 5mg/ml protein conc., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
