1RMO
Probing the Role of Tryptophans in Aequorea Victoria Green Fluorescent Proteins with an Expanded Genetic Code
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 2001-10-10 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.793, 62.773, 70.536 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 17.690 - 1.800 |
| R-factor | 0.1851 |
| Rwork | 0.185 |
| R-free | 0.22100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1emg |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.435 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 17.690 | 1.890 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Number of reflections | 20540 | |
| Completeness [%] | 93.7 | 92.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 14% PEG 1000, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
