5D7I
Structure of human MR1-Ac-6-FP in complex with human MAIT M33.64 TCR
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-03-22 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.954 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 214.300, 69.660, 141.190 |
Unit cell angles | 90.00, 103.99, 90.00 |
Refinement procedure
Resolution | 51.740 - 2.000 |
R-factor | 0.1798 |
Rwork | 0.178 |
R-free | 0.22010 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4l4t |
RMSD bond length | 0.007 |
RMSD bond angle | 1.086 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 51.740 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 133791 | |
<I/σ(I)> | 8.7 | 1.2 |
Completeness [%] | 98.1 | 97 |
Redundancy | 3.7 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 294 | BTP, PEG 3350, NaAc |