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 |
