3LVD
Crystal structure of GFP-like protein aceGFP_G222E (A. coerulescens). UV-photoconverted green form.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 59.472, 80.202, 95.370 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.388 - 1.751 |
| R-factor | 0.161 |
| Rwork | 0.160 |
| R-free | 0.19300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.986 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 1.810 |
| High resolution limit [Å] | 1.750 | 3.770 | 1.750 |
| Rmerge | 0.084 | 0.042 | 0.583 |
| Number of reflections | 46670 | ||
| <I/σ(I)> | 10.6 | ||
| Completeness [%] | 100.0 | 99.9 | 100 |
| Redundancy | 4.8 | 4.6 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 0.1M Bis-Tris, 25% PEG 3350, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |






