5E8P
The structure of the TEIPP associated altered peptide ligand Trh4-p5NLE in complex with H-2D(b)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-03-13 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.96500 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 90.590, 123.772, 97.683 |
| Unit cell angles | 90.00, 104.31, 90.00 |
Refinement procedure
| Resolution | 31.802 - 2.000 |
| R-factor | 0.2166 |
| Rwork | 0.214 |
| R-free | 0.25750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1s7u |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.190 |
| 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] | 32.300 | 2.040 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.080 | 0.340 |
| Number of reflections | 68583 | |
| <I/σ(I)> | 4.2 | 1.8 |
| Completeness [%] | 96.5 | 98.3 |
| Redundancy | 2.5 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 277 | 1.6 M ammonium sulphate, 0.1 M Tris-HCl, 0.5 M NaCl |
