3A8S
Crystal structure analysis of the fluorescent protein KillerRed
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2009-08-04 |
| Detector | RIGAKU RAXIS VII |
| Wavelength(s) | 2.29 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 123.464, 123.464, 110.171 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.880 - 2.900 |
| R-factor | 0.24737 |
| Rwork | 0.245 |
| R-free | 0.29818 |
| Structure solution method | SAD |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.913 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXDE |
| Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.950 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.072 | 0.350 |
| Number of reflections | 21805 | |
| <I/σ(I)> | 74.5 | 13.9 |
| Completeness [%] | 97.8 | 96.5 |
| Redundancy | 19.7 | 19.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.1 | 293 | 100mM MES pH6.1, 37.5% PEG 400, 5% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
