4LQT
1.10A resolution crystal structure of a superfolder green fluorescent protein (W57A) mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-11-14 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.8265 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 69.358, 46.433, 76.689 |
| Unit cell angles | 90.00, 105.58, 90.00 |
Refinement procedure
| Resolution | 24.704 - 1.100 |
| R-factor | 0.1348 |
| Rwork | 0.134 |
| R-free | 0.14560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2b3p |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.278 |
| Data reduction software | XDS |
| Data scaling software | SCALA (0.1.27) |
| Phasing software | PHASER (2.5.3) |
| Refinement software | PHENIX (dev_1228) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.885 | 1.120 |
| High resolution limit [Å] | 1.100 | 1.100 |
| Rmerge | 0.045 | 0.561 |
| Number of reflections | 93517 | |
| <I/σ(I)> | 12.1 | 1.9 |
| Completeness [%] | 98.3 | 98.4 |
| Redundancy | 3.4 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6.5 | 293 | 40% (v/v) Isopropanol, 0.1 M Imidazole acid, 15% (w/v) PEG 8000, pH 6.5, vapor diffusion, temperature 293K |
