7UGT
Crystal structure of hyperfolder fluorescent protein FOLD6
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-12-13 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 1.0332 |
| Spacegroup name | P 64 |
| Unit cell lengths | 61.438, 61.438, 112.380 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.632 - 1.210 |
| R-factor | 0.1465 |
| Rwork | 0.146 |
| R-free | 0.17100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5wj2 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.986 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.632 | 1.253 |
| High resolution limit [Å] | 1.210 | 1.210 |
| Rmerge | 0.037 | 1.128 |
| Rmeas | 0.041 | 1.552 |
| Rpim | 0.017 | 1.060 |
| Number of reflections | 117807 | 1788 |
| <I/σ(I)> | 18.36 | 0.36 |
| Completeness [%] | 87.9 | 24.56 |
| Redundancy | 4.8 | 1.2 |
| CC(1/2) | 1.000 | 0.290 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291.15 | 0.1 M Tris-HCl pH 8.5, 30% PEG 4000, 100 mM magnesium chloride |
