8BBH
The crystal structure of a mouse Fab fragment TL1 in complex with a human Glucose-6-phosphate isomerase peptide 293-307
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX IV BEAMLINE BioMAX |
Synchrotron site | MAX IV |
Beamline | BioMAX |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-09-26 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.97625 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 67.660, 75.545, 96.219 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 55.408 - 1.619 |
Rwork | 0.198 |
R-free | 0.22910 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | model structure |
RMSD bond length | 0.013 |
RMSD bond angle | 1.602 |
Data reduction software | XDS |
Data scaling software | XDS |
Refinement software | REFMAC (5.8.0349) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 55.408 | 8.870 |
High resolution limit [Å] | 1.619 | 1.620 |
Number of reflections | 63532 | 3127 |
<I/σ(I)> | 12.4 | |
Completeness [%] | 100.0 | |
Redundancy | 13.1 | |
CC(1/2) | 0.999 | 0.666 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 300 | 0.2 M Calcium acetate hydrate, 0.1 M Sodium cacodylate trihydrate pH 6.5, 18% w/v Polyethylene glycol 8,000 |