5E8N
The structure of the TEIPP associated Trh4 peptide 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 | CCD |
| Collection date | 2008-09-21 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9334 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 92.510, 124.250, 99.290 |
| Unit cell angles | 90.00, 103.26, 90.00 |
Refinement procedure
| Resolution | 52.259 - 2.250 |
| R-factor | 0.2416 |
| Rwork | 0.239 |
| R-free | 0.28630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1s7u |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.061 |
| 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] | 52.260 | 2.250 |
| High resolution limit [Å] | 2.240 | 2.240 |
| Rmerge | 0.084 | 0.430 |
| Number of reflections | 102342 | |
| <I/σ(I)> | 7.5 | 2.1 |
| Completeness [%] | 98.8 | 99.7 |
| Redundancy | 3.2 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 1.9 M Ammonium sulphate, 0.1 M Tris-HCl |
