2Q6P
The Chemical Control of Protein Folding: Engineering a Superfolder Green Fluorescent Protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-01-20 |
Detector | MARRESEARCH |
Wavelength(s) | 1.54 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.168, 62.556, 69.215 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.940 - 2.100 |
R-factor | 0.227 |
Rwork | 0.227 |
R-free | 0.26000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1emg |
RMSD bond length | 0.013 |
RMSD bond angle | 1.700 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.000 | 2.170 |
High resolution limit [Å] | 2.100 | 2.100 |
Number of reflections | 12901 | |
Completeness [%] | 95.8 | 98 |
Redundancy | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | PEG 8000, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |