2PSH
Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla Reniformis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.776, 75.652, 89.185 |
| Unit cell angles | 90.00, 76.48, 90.00 |
Refinement procedure
| Resolution | 86.710 - 1.790 |
| R-factor | 0.19698 |
| Rwork | 0.195 |
| R-free | 0.22941 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.212 |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 100.000 |
| High resolution limit [Å] | 1.790 |
| Number of reflections | 58344 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 0.1~M HEPES, 10% v/v isopropanol with 6mg/ml benzyl-coelenterazine, 15% w/v PEG 3350, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
