6AA7
Fluorescent protein from Acropora digitifera
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 11C |
| Synchrotron site | PAL/PLS |
| Beamline | 11C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-03-15 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.9794 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 78.618, 90.553, 73.429 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.170 - 1.800 |
| R-factor | 0.17811 |
| Rwork | 0.177 |
| R-free | 0.20752 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5y8q |
| RMSD bond length | 0.018 |
| RMSD bond angle | 2.023 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0218) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.010 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.067 | 0.375 |
| Rmeas | 0.071 | 0.375 |
| Rpim | 0.023 | 0.140 |
| Number of reflections | 49007 | 2426 |
| <I/σ(I)> | 33.05 | 2.88 |
| Completeness [%] | 99.5 | 99.3 |
| Redundancy | 8.1 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295.5 | HEPES, Lithium sulfate |
