5VLV
The apo form of the triclocarban-binding single domain camelid nanobody VHH T9
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-01-03 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 1.11583 |
| Spacegroup name | P 43 2 2 |
| Unit cell lengths | 48.814, 48.814, 119.280 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.810 - 1.350 |
| R-factor | 0.16314 |
| Rwork | 0.162 |
| R-free | 0.18887 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | T9 holo |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.395 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.810 | 1.390 |
| High resolution limit [Å] | 1.350 | 1.350 |
| Rmerge | 0.031 | 0.624 |
| Number of reflections | 32653 | |
| <I/σ(I)> | 24.5 | 2.4 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 6.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | protein concentration 40 mg/ml well 25% w/v PEG MME 3350, 200 mM ammonium sulfate, 100 mM Hepes |
