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 |