2YE1
X-ray structure of the cyan fluorescent proteinmTurquoise-GL (K206A mutant)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2010-07-21 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.140, 61.802, 69.814 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.260 - 1.630 |
| R-factor | 0.14819 |
| Rwork | 0.146 |
| R-free | 0.19389 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wso |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.348 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.6.0116) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.300 | 1.720 |
| High resolution limit [Å] | 1.630 | 1.630 |
| Rmerge | 0.060 | 0.670 |
| Number of reflections | 27133 | |
| <I/σ(I)> | 13.5 | 2 |
| Completeness [%] | 97.0 | 95.6 |
| Redundancy | 3.4 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 35 MG/ML PROTEIN, 14% PEG8000, 100 MM MGCL2, 100 MM HEPES PH 7.00 |
