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 |
