2O29
Spectroscopic and Structural Study of the Heterotropic Linkage between Halide and Proton Ion Binding to Gfp Proteins: E2(GFP)-BR Complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.144, 62.852, 69.172 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.150 - 1.800 |
R-factor | 0.17909 |
Rwork | 0.178 |
R-free | 0.20835 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2h6v |
RMSD bond length | 0.011 |
RMSD bond angle | 1.523 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.684 | 1.900 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.098 | 0.377 |
Number of reflections | 20873 | |
<I/σ(I)> | 6.9 | 2 |
Completeness [%] | 97.7 | 95.2 |
Redundancy | 5.2 | 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 NH4Br, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 100K |