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 |
