1EMG
GREEN FLUORESCENT PROTEIN (65-67 REPLACED BY CRO, S65T SUBSTITUTION, Q80R)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 295 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.733, 62.822, 70.517 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.19 * |
Rwork | 0.186 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ema |
RMSD bond length | 0.009 |
RMSD bond angle | 2.100 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | TNT |
Refinement software | TNT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.075 | |
Total number of observations | 93073 * | |
Number of reflections | 16011 | |
Completeness [%] | 99.0 | 94 |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.9 * | CRYSTALLIZATION CONDITIONS: 22-26% PEG 4000, 50 MM HEPES PH 8.0, 50 MM MGCL2, 12 MG PROTEIN |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 12 (mg/ml) | |
2 | 1 | drop | Tris | 20 (mM) | |
3 | 1 | reservoir | HEPES | 50 (mM) | |
4 | 1 | reservoir | 50 (mM) | ||
5 | 1 | reservoir | PEG4000 | 23-26 (%) |