6UD1
Spectroscopic and structural characterization of a genetically encoded direct sensor for protein-ligand interactions
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-08-18 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 1.000 |
| Spacegroup name | I 41 |
| Unit cell lengths | 57.351, 57.351, 172.320 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 86.160 - 1.550 |
| R-factor | 0.1674 |
| Rwork | 0.166 |
| R-free | 0.19180 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1swc |
| RMSD bond length | 0.027 |
| RMSD bond angle | 2.467 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 86.160 | 1.580 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Number of reflections | 400052 | 1924 |
| <I/σ(I)> | 14.3 | 2.3 |
| Completeness [%] | 99.9 | |
| Redundancy | 10.3 | |
| CC(1/2) | 0.999 | 0.794 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 3.5 | 298 | 500 ul of 0.1 M Citric Acid, pH 3.5, 3M NaCl in the reservoir with 2 ul of reservoir buffer mixed with 2 ul of 10 mg/ml of protein in the drop. Crystals were soaked to pH 5.5 overnight with 3 exchanges |
