2YE0
X-ray structure of the cyan fluorescent protein mTurquoise (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 | 2010-09-30 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.984, 62.320, 70.366 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.290 - 1.470 |
| R-factor | 0.14369 |
| Rwork | 0.141 |
| R-free | 0.18495 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wso |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.495 |
| 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] | 46.700 | 1.550 |
| High resolution limit [Å] | 1.470 | 1.470 |
| Rmerge | 0.040 | 0.750 |
| Number of reflections | 38321 | |
| <I/σ(I)> | 15.9 | 2 |
| Completeness [%] | 98.8 | 98.8 |
| Redundancy | 4.1 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.75 | 16 MG/ML PROTEIN, 14% PEG8000, 100 MM MGCL2, 100 MM HEPES PH 6.75 |
