2H6V
Spectroscopic and structural study of the heterotropic linkage between halide and proton ion binding to GFP proteins- E2(GFP) APO FORM
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.133, 62.850, 69.631 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.620 - 1.470 |
| R-factor | 0.16017 |
| Rwork | 0.159 |
| R-free | 0.18692 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.350 |
| Data reduction software | MOSFLM |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.700 | 1.540 |
| High resolution limit [Å] | 1.470 | 1.470 |
| Rmerge | 0.072 | 0.156 |
| Number of reflections | 38294 | |
| <I/σ(I)> | 5.6 | 4.1 |
| Completeness [%] | 75.0 | 95 |
| Redundancy | 7 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5 | 14% (w/v) PEG3350, 100 mM NH4 acetate pH 5.0, 0.2 M NH4F, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 100K |
