6OFL
Crystal structure of green fluorescent protein (GFP); S65T, Y66(3-ClY); ih circular permutant (50-51)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL14-1 |
| Synchrotron site | SSRL |
| Beamline | BL14-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-10-27 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.220, 68.730, 60.880 |
| Unit cell angles | 90.00, 100.57, 90.00 |
Refinement procedure
| Resolution | 36.520 - 1.250 |
| R-factor | 0.12834 |
| Rwork | 0.127 |
| R-free | 0.15837 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4zf3 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.616 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.520 | 1.280 |
| High resolution limit [Å] | 1.250 | 1.250 |
| Rmeas | 0.058 | 1.650 |
| Number of reflections | 113139 | 7995 |
| <I/σ(I)> | 27.4 | 1.5 |
| Completeness [%] | 96.9 | 93.6 |
| Redundancy | 23 | 10.9 |
| CC(1/2) | 1.000 | 0.721 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 295 | 0.15 M ammonium acetate, 30% PEG 3350 |
