25HK
Crystal structure of a TctC solute binding protein from Vibrio sp. C42, no ligand
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL02U1 |
| Synchrotron site | SSRF |
| Beamline | BL02U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-06-10 |
| Detector | DECTRIS EIGER2 S 9M |
| Wavelength(s) | 1.802 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 65.414, 89.895, 95.951 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 54.050 - 1.660 |
| R-factor | 0.2085 |
| Rwork | 0.207 |
| R-free | 0.23510 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.780 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 54.050 | 1.700 |
| High resolution limit [Å] | 1.660 | 1.660 |
| Rmerge | 0.077 | |
| Number of reflections | 66738 | 3384 |
| <I/σ(I)> | 17.5 | |
| Completeness [%] | 98.8 | |
| Redundancy | 10.6 | |
| CC(1/2) | 0.999 | 0.860 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 292 | 30% (w/v) PEG 1500, 0.1 M BICINE pH 8.5, and 2% (v/v) 2-propanol |
