5E8O
The structure of the TEIPP associated altered peptide ligand Trh4-p2ABU in complex with H-2D(b)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-01-29 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.9184 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 90.859, 123.330, 97.552 |
| Unit cell angles | 90.00, 104.67, 90.00 |
Refinement procedure
| Resolution | 32.329 - 1.980 |
| R-factor | 0.2198 |
| Rwork | 0.218 |
| R-free | 0.25390 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1s7u |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.960 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.329 | 2.020 |
| High resolution limit [Å] | 1.980 | 1.980 |
| Rmerge | 0.100 | 0.700 |
| Number of reflections | 71202 | |
| <I/σ(I)> | 9 | 2 |
| Completeness [%] | 98.6 | 97.9 |
| Redundancy | 6.2 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 1.5 M ammonium sulphate, 0.1 M Tris-HCl, 0.5 M NaCl |
