1LK2
1.35A crystal structure of H-2Kb complexed with the GNYSFYAL peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-1 |
| Synchrotron site | SSRL |
| Beamline | BL9-1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-02-13 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.970 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 135.549, 87.650, 45.118 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.350 - 1.350 |
| R-factor | 0.15023 |
| Rwork | 0.149 |
| R-free | 0.16400 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.190 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.370 |
| High resolution limit [Å] | 1.350 | 1.350 |
| Rmerge | 0.053 * | 0.813 * |
| Number of reflections | 117515 | 5606 * |
| <I/σ(I)> | 23.95 | 1.13 |
| Completeness [%] | 98.9 | 95.3 |
| Redundancy | 3.4 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291 | Stura, E.A., (1992) J. Mol. Biol., 228, 975. * |
