2H9W
Green fluorescent protein ground states: the influence of a second protonation site near the chromophore
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 298 |
Detector technology | CCD |
Collection date | 2006-03-01 |
Detector | MARRESEARCH |
Wavelength(s) | 0.979469 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.886, 62.933, 71.035 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.090 - 1.820 |
R-factor | 0.16732 |
Rwork | 0.166 |
R-free | 0.18594 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2h6v |
RMSD bond length | 0.011 |
RMSD bond angle | 1.578 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CCP4 |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.106 | 1.920 |
High resolution limit [Å] | 1.820 | 1.820 |
Rmerge | 0.066 | 0.387 |
Number of reflections | 20710 | |
<I/σ(I)> | 8.2 | 1.9 |
Completeness [%] | 97.2 | 97.2 |
Redundancy | 6.3 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 298 | AS, Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |