1K5N
HLA-B*2709 BOUND TO NONA-PEPTIDE M9
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-06-17 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9393 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.845, 82.484, 110.708 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.100 - 1.090 |
| R-factor | 0.12349 |
| Rwork | 0.123 |
| R-free | 0.14800 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1JGE (HLA-B*2705:m9) with Asp-A116 truncated to Ala |
| RMSD bond length | 0.022 |
| RMSD bond angle | 2.260 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.100 | 1.120 |
| High resolution limit [Å] | 1.090 | 1.090 |
| Rmerge | 0.091 | 0.376 |
| Number of reflections | 187545 | 12377 * |
| <I/σ(I)> | 12.8 | 2.9 |
| Completeness [%] | 96.7 | 96.8 |
| Redundancy | 4.7 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 291 | used cross-seeding * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 2 | 1 | drop | Tris | 20 (mM) | pH7.5 |
| 3 | 1 | drop | 150 (mM) | ||
| 4 | 1 | reservoir | PEG8000 | 28 (%) |
