4H25
TCR interaction with peptide mimics of nickel offers structure insights to nickel contact allergy
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 154.520, 97.180, 67.100 |
| Unit cell angles | 90.00, 105.36, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.200 |
| R-factor | 0.22 |
| Rwork | 0.210 |
| R-free | 0.25500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | THE RFREE VALUE PROVIDED BY AUTHORS CAN NOT BE REPRODUCED BASED ON THE RFREE FLAGS PROVIDED BY AUTHORS |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASES |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 40.000 |
| High resolution limit [Å] | 2.200 |
| Number of reflections | 48623 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 16% PEG4000, 100mM Tris-HCL, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
