4B5Y
X-ray structure of the cyan fluorescent protein mTurquoise-GL (K206A mutant) in space group C222(1)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-10-01 |
| Detector | ADSC CCD |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 60.731, 92.481, 117.576 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.420 - 1.450 |
| R-factor | 0.1471 |
| Rwork | 0.145 |
| R-free | 0.17878 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wso |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.654 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0116) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.600 | 1.530 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.060 | 0.500 |
| Number of reflections | 57436 | |
| <I/σ(I)> | 10 | 2 |
| Completeness [%] | 97.7 | 99.7 |
| Redundancy | 3.4 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 35 MG/ML PROTEIN, 14% PEG8000, 100 MM MGCL2, 100 MM HEPES PH 6.50 |
