3LN5
Crystal structure of HLA-B*4104 in complex with a 11mer self-peptide derived from S-methyl-5-thioadenosine phosphorylase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-02-22 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.98133 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.950, 82.120, 110.210 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.044 - 1.900 |
| R-factor | 0.1957 |
| Rwork | 0.191 |
| R-free | 0.24100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1syv |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.004 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 55.100 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.071 | 0.455 |
| Number of reflections | 35909 | |
| <I/σ(I)> | 16.79 | 4.26 |
| Completeness [%] | 96.5 | 88.9 |
| Redundancy | 4 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 294 | 0.1M citrate pH 5.6, 14-20% PEG 4000, 0.2M NH4OAc, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
