2O24
Spectroscopic and Structural Study of the Heterotropic Linkage between Halide and Proton Ion Binding to Gfp Proteins: E2(GFP)-Cl Complex
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 | 50.989, 62.979, 69.390 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.680 - 1.450 |
| R-factor | 0.17805 |
| Rwork | 0.177 |
| R-free | 0.19157 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2h6v |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.400 |
| Data reduction software | MOSFLM |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.684 | 1.530 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.074 | 0.338 |
| Number of reflections | 38294 | |
| <I/σ(I)> | 5.8 | 2.2 |
| Completeness [%] | 97.0 | 95.8 |
| Redundancy | 7.1 | 6.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 14% (W/V) PEG 3350, 100 MM NH4 ACETATE, 0.2 M NH4CL, PH 5.0, VAPOR DIFFUSION, HANGING DROP |
