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 |