5EHU
sfGFP mutant with unnatural amino acid 4-azidoethoxy-L-phenylalanine incorporated at the 149 site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-04-02 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 129.917, 37.492, 91.848 |
| Unit cell angles | 90.00, 106.31, 90.00 |
Refinement procedure
| Resolution | 45.262 - 1.450 |
| R-factor | 0.1756 |
| Rwork | 0.175 |
| R-free | 0.20830 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2b3p |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.357 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.480 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.089 | 0.385 |
| Number of reflections | 73332 | |
| <I/σ(I)> | 16.5 | 1.9 |
| Completeness [%] | 96.4 | 94.3 |
| Redundancy | 3.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | A 40 mg/mL solution of sfGFP-149-AePhe in a 20 mM Hepes buffer pH 7.5 was combined with a precipitation solution (20% PEG 8000, 100 mM Hepes pH 7.5) in a 1:1 ratio to form crystals in a sitting drop well at room temperature |
